Structure of PDB 5jy6 Chain D

Receptor sequence
>5jy6D (length=333) Species: 1311 (Streptococcus agalactiae) [Search protein sequence]
VKVGINGFGRIGRLAFRRIQNVEGVEVTRINDLTDPNMLAHLLKYDTTQG
RFDGTVEVKEGGFEVNGQFVKVSAEREPANIDWATDGVEIVLEATGFFAS
KEKAEQHIHENGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASC
TTNCLAPMAKALQDNFGVKQGLMTTIHAYTGDQMILDGPHRGGDLRRARA
GAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVATLEK
DVTVEEVNAAMKAAANDSYGYTEDPIVSSDIVGISYGSLFDATQTKVQTV
DGNQLVKVVSWYDNEMSYTSQLVRTLEYFAKIA
3D structure
PDB5jy6 Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes.
ChainD
Resolution2.0 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) C150 H177
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 D G9 G11 R12 I13 D34 L35 A96 T97 G98 F99 F100 T121 C152 N316 Y320 G7 G9 R10 I11 D32 L33 A94 T95 G96 F97 F98 T119 C150 N314 Y318
BS02 MG D I21 V24 V27 I19 V22 V25
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:5jy6, PDBe:5jy6, PDBj:5jy6
PDBsum5jy6
PubMed27875551
UniProtQ9ALW2

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