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4G5D

X-ray crystal structure of Prostaglandin f synthase from Leishmania major Friedlin bound to NADPH

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001516biological_processprostaglandin biosynthetic process
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
A0044281biological_processsmall molecule metabolic process
B0000166molecular_functionnucleotide binding
B0001516biological_processprostaglandin biosynthetic process
B0004033molecular_functionaldo-keto reductase (NADPH) activity
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
B0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues35
DetailsBINDING SITE FOR RESIDUE NDP A 301
ChainResidue
AGLY23
AGLN171
ATRP197
ASER198
APRO199
ALEU200
AGLY201
AGLN202
AGLY203
ALEU206
AILE238
AVAL24
APRO239
ALYS240
ASER241
AVAL242
AHIS243
AARG246
AGLU249
AASN250
AHOH427
AHOH434
ATRP25
AHOH436
AHOH437
AHOH439
AHOH440
AHOH546
AHOH573
AASP49
ATYR54
AHIS112
ATRP113
ASER149
AASN150

site_idAC2
Number of Residues37
DetailsBINDING SITE FOR RESIDUE NDP B 301
ChainResidue
BGLY23
BVAL24
BTRP25
BASP49
BTYR54
BLYS79
BHIS112
BSER149
BASN150
BGLN171
BTRP197
BSER198
BPRO199
BLEU200
BGLY201
BGLN202
BGLY203
BLEU206
BALA223
BILE238
BPRO239
BLYS240
BSER241
BVAL242
BHIS243
BARG246
BGLU249
BASN250
BHOH437
BHOH440
BHOH441
BHOH564
BHOH568
BHOH586
BHOH599
BHOH632
BHOH786

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. FeqlykekkVRAIGVSNF
ChainResidueDetails
APHE134-PHE151

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVHreRIeENaDI
ChainResidueDetails
AILE238-ILE253

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAaiyknEesVG
ChainResidueDetails
AGLY44-GLY61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR54
BTYR54

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS112
ASER149
AGLN171
ATRP197
ALYS240
AARG246
BVAL24
BASP49
BHIS112
BSER149
BGLN171
BTRP197
BLYS240
BARG246
AVAL24
AASP49

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS79
BLYS79

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PDB entries from 2024-06-12

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