Structure of PDB 7c5q Chain Q

Receptor sequence
>7c5qQ (length=333) Species: 469008 (Escherichia coli BL21(DE3)) [Search protein sequence]
MSKVGINGFGRIGRLVLRRLLEVKSNIDVVAINDLTSPKILAYLLKHDSN
YGPFPWSVDFTEDSLIVDGKSIAVYAEKEAKNIPWKAKGAEIIVECTGFY
TSAEKSQAHLDAGAKKVLISAPAGEMKTIVYNVNDDTLDGNDTIVSVASC
TTNCLAPMAKALHDSFGIEVGTMTTIAAYTGTQSLVDGPRGKDLRASRAA
AENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGSVTELVSILGKK
VTAEEVNNALKQATTNNESFGYTDEEIVSSDIIGSHFGSVFDATQTEITA
VGDLQLVKTVAWYDNEYGFVTQLIRTLEKFAKL
3D structure
PDB7c5q Novel Structures of Type 1 Glyceraldehyde-3-phosphate Dehydrogenase from Escherichia coli Provide New Insights into the Mechanism of Generation of 1,3-Bisphosphoglyceric Acid.
ChainQ
Resolution2.13 Å
3D
structure
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Enzymatic activity
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 Q G8 G10 R11 I12 D34 L35 K78 C96 T97 F99 S120 C150 N315 F319 G8 G10 R11 I12 D34 L35 K78 C96 T97 F99 S120 C150 N315 F319
BS02 G3H Q T180 G181 T182 T180 G181 T182
BS03 PO4 Q H163 G167 I168 K225 H163 G167 I168 K225
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: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:7c5q, PDBe:7c5q, PDBj:7c5q
PDBsum7c5q
PubMed34827563
UniProtA0A140NCK4

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