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4E15

Crystal structure of kynurenine formamidase conjugated with an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004061molecular_functionarylformamidase activity
A0006569biological_processtryptophan catabolic process
A0016787molecular_functionhydrolase activity
A0019441biological_processtryptophan catabolic process to kynurenine
B0004061molecular_functionarylformamidase activity
B0006569biological_processtryptophan catabolic process
B0016787molecular_functionhydrolase activity
B0019441biological_processtryptophan catabolic process to kynurenine
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
ALEU119
ACYS120
APRO121
AGLN122
AHOH576
AHOH594

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
ALYS265
ASER267
ALYS235
AILE236
ATYR237

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
ATHR76
AASN77
ASER197
ALEU199
AGLU200
AASN203

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
APHE36
AHIS86
AGLY87
AMET93
AMET97
ASER98
AHIS156

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 401
ChainResidue
BPHE36
BHIS86
BGLY87
BMET93
BMET97
BSER98
BHIS156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_03014
ChainResidueDetails
ASEB157
BSEB157

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_03014
ChainResidueDetails
AASP244
AHIS276
BASP244
BHIS276

220113

PDB entries from 2024-05-22

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