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4F40

X-ray crystal structure of Apo prostaglandin f synthase from Leishmania major Friedlin

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 Residues13
DetailsBINDING SITE FOR RESIDUE CIT A 301
ChainResidue
AGLY14
AHOH476
AHOH492
AHOH596
AHOH620
ALYS16
ATRP25
AGLN26
AEDO303
AEDO305
AEDO308
AHOH414
AHOH449

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
APRO18
AGLU72
AASP73
AHOH450
AHOH526
AHOH698

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AGLY14
ALYS16
ATRP25
APRO277
ACIT301
AHOH492
AHOH630

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AASP118
ACYS163
ATHR164
ATHR166
AGLN283
AHOH677

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AASN13
AGLY14
AVAL15
ATRP81
APHE284
ACIT301
AHOH492
AHOH568

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AHIS154
AGLU157
AASP158
AHOH446
AHOH474

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
AALA52
ATRP81
AGLU84
AHOH438
AHOH506

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
ATRP25
ATYR54
AHIS112
AASN150
ATRP197
ACIT301
AHOH473

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 309
ChainResidue
ATYR138
ALYS141
AHOH523
AHOH534
AHOH559
AHOH588
AHOH629

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 310
ChainResidue
ASER198
APRO199
ALEU200
AGLY201
APRO239
ALYS240

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 311
ChainResidue
AALA260
AGLU261
AHOH462

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT B 301
ChainResidue
BGLY14
BLYS16
BTRP25
BGLN26
BEDO302
BEDO307
BHOH422
BHOH442
BHOH478
BHOH499
BHOH669
BHOH698

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BGLY14
BLYS16
BTRP25
BPRO277
BCIT301
BHOH601
BHOH698

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
BGLU72
BHOH446
BHOH525
BHOH568
BHOH694

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BTRP81
BPHE284
BHOH517
BHOH636
BHOH698
BHOH720
BASN13
BGLY14

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
BTYR138
BHOH475
BHOH479
BHOH490
BHOH560
BHOH585

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 306
ChainResidue
BLYS240
BSER241
BVAL242
BHIS243

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 307
ChainResidue
BTRP25
BTYR54
BHIS112
BASN150
BTRP197
BCIT301
BHOH465

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 308
ChainResidue
BTHR271
BSER273
BHOH489
BHOH686

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 309
ChainResidue
BARG228
BPHE254

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 310
ChainResidue
BALA52
BTRP81
BGLU84
BHOH421

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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