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1EVZ

CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0020015cellular_componentglycosome
A0046168biological_processglycerol-3-phosphate catabolic process
A0047952molecular_functionglycerol-3-phosphate dehydrogenase [NAD(P)+] activity
A0051287molecular_functionNAD binding
A0141152molecular_functionglycerol-3-phosphate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAD A 400
ChainResidue
ASER23
ATHR124
ALYS125
ASER155
AALA157
AGLU300
AHOH559
AGLY24
AALA25
APHE26
AHIS45
AMET46
APHE63
APRO94
APHE97

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MYS A 500
ChainResidue
AVAL219
AALA220
ALEU342
ACYS345

Functional Information from PROSITE/UniProt
site_idPS00957
Number of Residues22
DetailsNAD_G3PDH NAD-dependent glycerol-3-phosphate dehydrogenase signature. SAVKNVLAiGsGVanGLgMGlN
ChainResidueDetails
ASER207-ASN228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10801498","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12758080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12758080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1evy
ChainResidueDetails
ALYS210
ATHR267

site_idMCSA1
Number of Residues2
DetailsM-CSA 593
ChainResidueDetails
ALYS210proton acceptor, proton donor
ATHR267electrostatic stabiliser

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PDB entries from 2025-08-27

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