Structure of PDB 5jya Chain A

Receptor sequence
>5jyaA (length=330) Species: 1311 (Streptococcus agalactiae) [Search protein sequence]
VKVGINGFGRIGRLAFRRIQNVEGVEVTRINDLTDPNMLAHLLKYDTTQG
RFDGTVEVKEGGFEVNGQFVKVSAEREPANIDWATDGVEIVLEATGFFAS
KEKAEQHIHEGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASST
TNCLAPMAKALQDNFGVKQGLMTTIHAYTGDQMILDGPHRGGDLRRARAG
AANIVPNSTGAAIGLVIPELNGKLDGAAQRVPVPTGSVTELVATLEKDVT
VEEVNAAMKAAANDSYGYTEDPIVSSDIVGISYGSLFDATQTKVQTVDGN
QLVKVVSWYDNEMSYTSQLVRTLEYFAKIA
3D structure
PDB5jya Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes.
ChainA
Resolution2.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S152 H179
Catalytic site (residue number reindexed from 1) S149 H176
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 A G11 R12 I13 D34 L35 T97 G98 F99 T121 S152 N316 Y320 G9 R10 I11 D32 L33 T95 G96 F97 T118 S149 N311 Y315
BS02 G3H A S151 S152 T153 H179 G213 S148 S149 T150 H176 G210
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:0042802 identical protein binding
GO:0046872 metal ion 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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External links
PDB RCSB:5jya, PDBe:5jya, PDBj:5jya
PDBsum5jya
PubMed27875551
UniProtQ9ALW2

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