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1EVY

CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006072biological_processglycerol-3-phosphate metabolic process
A0006116biological_processNADH oxidation
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
A0051287molecular_functionNAD binding
A0141152molecular_functionglycerol-3-phosphate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MYS A 500
ChainResidue
ATRP195
AALA220
AILE328
ALEU342
ACYS345
AHOH704

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
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
ALYS210

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10801498, ECO:0000269|PubMed:12758080
ChainResidueDetails
AGLY22
AALA157
AVAL298
AGLU300

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
APHE97
AARG274

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12758080
ChainResidueDetails
ALYS125

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 12758080, 10801498
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 2024-10-30

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