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4GIE

Crystal structure of prostaglandin F synthase from Trypanosoma cruzi bound to NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001516biological_processprostaglandin biosynthetic process
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0036130molecular_functionprostaglandin H2 endoperoxidase reductase activity
A0044281biological_processsmall molecule metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 301
ChainResidue
ATRP24
ATYR53
AHIS111
ATRP112
ANAP302
AHOH562

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE NAP A 302
ChainResidue
AASP48
ATYR53
AHIS111
ATRP112
ASER140
AASN141
AGLN162
ATRP188
ASER189
APRO190
ALEU191
AGLY192
ASER193
AGLY194
ALEU200
AALA217
AILE232
APRO233
ALYS234
ASER235
ATHR236
AARG240
AGLU243
AASN244
AACT301
AHOH405
AHOH471
AHOH588
AHOH598
AHOH602
AHOH637
AHOH658
AHOH684
AHOH757
AHOH762
AGLY22
AVAL23
ATRP24

Functional Information from PROSITE/UniProt
site_idPS00062
Number of Residues18
DetailsALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeklyeekkVRAIGVSNF
ChainResidueDetails
ALEU125-PHE142

site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSTNkgRIqENfNV
ChainResidueDetails
AILE232-VAL247

site_idPS00798
Number of Residues18
DetailsALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDTAyiysnErgVG
ChainResidueDetails
AGLY43-GLY60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ATYR53

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL23
AASP48
AHIS111
ASER140
AGLN162
ATRP188
ALYS234
AARG240

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Lowers pKa of active site Tyr => ECO:0000250
ChainResidueDetails
ALYS78

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PDB entries from 2024-07-24

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