GlycoNAVI Proteins

GlycoNAVI-Proteins is dataset of glycan and protein information. This is the content of GlycoNAVI.

Source Last Updated
GlycoNAVI Proteins September 04, 2024
Displaying entries 17001 - 17050 of 39437 in total
PDB ID UniProt ID ▲ Title Descriptor
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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Last updated: August 19, 2024