Structure of PDB 4qx6 Chain B

Receptor sequence
>4qx6B (length=335) Species: 211110 (Streptococcus agalactiae NEM316) [Search protein sequence]
VVKVGINGFGRIGRLAFRRIQNVEGVEVTRINDLTDPNMLAHLLKYDTTQ
GRFDGTVEVKEGGFEVNGQFVKVSAEREPANIDWATDGVEIVLEATGFFA
SKEKAEQHIHENGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGAS
CTTNCLAPMAKALQDNFGVKQGLMTTIHAYTGDQMILDGPHRGGDLRRAR
AGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVATLE
KDVTVEEVNAAMKAAANDSYGYTEDPIVSSDIVGISYGSLFDATQTKVQT
VDGNQLVKVVSWYDNEMSYTSQLVRTLEYFAKIAK
3D structure
PDB4qx6 Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.
ChainB
Resolution2.46 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C152 H179
Catalytic site (residue number reindexed from 1) C151 H178
Enzyme Commision number 1.2.1.-
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 B G11 R12 I13 D34 L35 R78 A96 T97 G98 F99 F100 T121 C152 N316 Y320 G10 R11 I12 D33 L34 R77 A95 T96 G97 F98 F99 T120 C151 N315 Y319
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:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0006006 glucose metabolic 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:4qx6, PDBe:4qx6, PDBj:4qx6
PDBsum4qx6
PubMed25286935
UniProtQ8E3E8

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