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2HKI

Crystal structure of photosynthetic glyceraldehyde-3-phosphate dehydrogenase A4 isoform

Functional Information from GO Data
ChainGOidnamespacecontents
A0006006biological_processglucose metabolic process
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ASER152
ATHR154
ATHR211
AGLY212
AALA213

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
ATHR183
AASP185
AARG198
AARG234

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AARG187
ASER192
ASO4504

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AGLY10
AARG11
AILE12
ASO4503

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA151-LEU158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS153

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11846565, ECO:0000269|PubMed:12705826, ECO:0000269|PubMed:15236965, ECO:0000269|PubMed:17573533
ChainResidueDetails
AARG11
AASP35
AARG80
AASN316

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER152
ATHR183
AARG198
ATHR211
AARG234

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Activates thiol group during catalysis => ECO:0000250
ChainResidueDetails
AHIS180

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
AHIS180
ACYS153

226707

PDB entries from 2024-10-30

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