GlycoNAVI-Proteins is dataset of glycan and protein information. This is the content of GlycoNAVI.
Source | Last Updated |
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GlycoNAVI Proteins | September 04, 2024 |
PDB ID | UniProt ID ▲ | Title | Descriptor |
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1RSC | P04716 | STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE | |
1UZH | P04716 | A CHIMERIC CHLAMYDOMONAS, SYNECHOCOCCUS RUBISCO ENZYME | |
4HHH | P04717 | Structure of Pisum sativum Rubisco | Ribulose bisphosphate carboxylase large chain (E.C.4.1.1.39), Pea Ribulose-1,5-bisphosphate carboxylase oxygenase - small subunit |
4MKV | P04717 | Structure of Pisum sativum Rubisco with ABA | Ribulose bisphosphate carboxylase large chain (E.C.4.1.1.39), Ribulose bisphosphate carboxylase small chain 3A, chloroplastic (E.C.4.1.1.39) |
9RUB | P04718 | CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE COMPLEXED WITH ITS SUBSTRATE, RIBULOSE-1,5-BISPHOSPHATE | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGLUCOSE (RUBISCO) (E.C.4.1.1.39) COMPLEXED WITH CO2, MG++, AND SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE |
5HQM | P04718 | Structure function studies of R. palustris RubisCO (R. palustris/R. rubrum chimera) | |
1MFU | P04745 | Probing the role of a mobile loop in human salivary amylase: Structural studies on the loop-deleted mutant | |
1MFV | P04745 | Probing the role of a mobile loop in human slaivary amylase: Structural studies on the loop-deleted enzyme | Alpha-amylase, salivary |
1NM9 | P04745 | Crystal structure of recombinant human salivary amylase mutant W58A | |
1Z32 | P04745 | Structure-function relationships in human salivary alpha-amylase: Role of aromatic residues | |
3BLK | P04745 | Role of aromatic residues in starch binding | |
3BLP | P04745 | Role of aromatic residues in human salivary alpha-amylase | |
3DHP | P04745 | Probing the role of aromatic residues at the secondary saccharide binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding | |
6OCN | P04746 | Montbretin A analogue M06-MbA in complex with Human pancreatic alpha-amylase | |
5TD4 | P04746 | Starch binding sites on the Human pancreatic alpha amylase D300N variant complexed with an octaose substrate. | |
5U3A | P04746 | Ultra High Resolution Crystal Structure of Human Pancreatic Alpha Amylase | |
1B2Y | P04746 | STRUCTURE OF HUMAN PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE CARBOHYDRATE INHIBITOR ACARBOSE | |
1BSI | P04746 | HUMAN PANCREATIC ALPHA-AMYLASE FROM PICHIA PASTORIS, GLYCOSYLATED PROTEIN | ALPHA-AMYLASE |
6Z8L | P04746 | Alpha-Amylase in complex with probe fragments | |
6OBX | P04746 | Montbretin A analogue M10-MbA in complex with Human pancreatic alpha-amylase | |
1CPU | P04746 | SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT | |
1KB3 | P04746 | Three Dimensional Structure Analysis of the R195A Variant of Human Pancreatic Alpha Amylase | |
1KBK | P04746 | Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids | |
1KGW | P04746 | THREE DIMENSIONAL STRUCTURE ANALYSIS OF THE R337Q VARIANT OF HUMAN PANCREATIC ALPHA-MYLASE | |
1KGX | P04746 | Three Dimensional Structure Analysis of the R195Q Variant of Human Pancreatic Alpha Amylase | |
1U2Y | P04746 | In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing D-gluconhydroximo-1,5-lactam | Alpha-amylase, pancreatic (E.C.3.2.1.1) |
1U30 | P04746 | In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D-gluconhydroximo-1,5-lactam | Alpha-amylase, pancreatic (E.C.3.2.1.1) |
1U33 | P04746 | In situ extension as an approach for identifying novel alpha-amylase inhibitors | Alpha-amylase, pancreatic (E.C.3.2.1.1) |
1XCW | P04746 | Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts | Alpha-amylase (E.C.3.2.1.1) |
1XCX | P04746 | Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts | Alpha-amylase, pancreatic precursor (E.C.3.2.1.1) |
1XD0 | P04746 | Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts | Alpha-amylase (E.C.3.2.1.1) |
1XD1 | P04746 | Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts | Alpha-amylase (E.C.3.2.1.1) |
1XGZ | P04746 | Structure of the N298S variant of human pancreatic alpha-amylase | |
1XH0 | P04746 | Structure of the N298S variant of human pancreatic alpha-amylase complexed with acarbose | |
1XH1 | P04746 | Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride | |
1XH2 | P04746 | Structure of the N298S variant of human pancreatic alpha-amylase complexed with chloride and acarbose | |
2QMK | P04746 | Human pancreatic alpha-amylase complexed with nitrite | |
2QV4 | P04746 | Human pancreatic alpha-amylase complexed with nitrite and acarbose | |
3BAI | P04746 | Human Pancreatic Alpha Amylase with Bound Nitrate | |
3BAJ | P04746 | Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose | |
3BAK | P04746 | N298S mutant of Human Pancreatic Alpha-Amylase in complex with nitrate | |
3BAW | P04746 | Human pancreatic alpha-amylase complexed with azide | Pancreatic alpha-amylase (E.C.3.2.1.1) |
3BAX | P04746 | N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide | |
3BAY | P04746 | N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Nitrate and Acarbose | |
3CPU | P04746 | SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT | |
3IJ7 | P04746 | Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase | Pancreatic alpha-amylase (E.C.3.2.1.1) |
3IJ8 | P04746 | Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase | Pancreatic alpha-amylase (E.C.3.2.1.1) |
3IJ9 | P04746 | Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase | Pancreatic alpha-amylase (E.C.3.2.1.1) |
3OLD | P04746 | Crystal structure of alpha-amylase in complex with acarviostatin I03 | |
3OLE | P04746 | Structures of human pancreatic alpha-amylase in complex with acarviostatin II03 |
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Supported by JST NBDC Grant Number JPMJND2204
Partly supported by NIH Common Fund Grant #1U01GM125267-01
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Last updated: August 19, 2024