Structure of PDB 3vaz Chain A

Receptor sequence
>3vazA (length=334) Species: 282458 (Staphylococcus aureus subsp. aureus MRSA252) [Search protein sequence]
AVKVAINGFGRIGRLAFRRIQEVEGLEVVAVNDLTDDDMLAHLLKYDTMQ
GRFTGEVEVVDGGFRVNGKEVKSFSEPDASKLPWKDLNIDVVLECTGFYT
DKDKAQAHIEAGAKKVLISAPATGDLKTIVFNTNHQELDGSETVVSGASC
TTNSLAPVAKVLNDDFGLVEGLMTTIHAYTGDQNTQDAPHRKGDKRRARA
AAENIIPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGSLTELTVVLEK
QDVTVEQVNEAMKNASNESFGYTEDEIVSSDVVGMTYGSLFDATQTRVMS
VGDRQLVKVAAWYDNEMSYTAQLVRTLAYLAELS
3D structure
PDB3vaz Crystal structure of Staphylococcal GAPDH1 in a hexagonal space group
ChainA
Resolution3.19 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C151 H178
Catalytic site (residue number reindexed from 1) C150 H177
Enzyme Commision number 1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 NAD A G11 R12 I13 D34 L35 T97 F99 S120 C151 N316 Y320 G10 R11 I12 D33 L34 T96 F98 S119 C150 N315 Y319
BS02 DGY A D165 D166 F167 D164 D165 F166
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0030554 adenyl nucleotide binding
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006096 glycolytic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3vaz, PDBe:3vaz, PDBj:3vaz
PDBsum3vaz
PubMed
UniProtQ6GIL8|G3P1_STAAR Glyceraldehyde-3-phosphate dehydrogenase 1 (Gene Name=gapA1)

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