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4E11

Crystal structure of kynurenine formamidase from Drosophila melanogaster

Functional Information from GO Data
ChainGOidnamespacecontents
A0004061molecular_functionarylformamidase activity
A0006569biological_processL-tryptophan catabolic process
A0016787molecular_functionhydrolase activity
A0019441biological_processL-tryptophan catabolic process to kynurenine
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 401
ChainResidue
AGLY88
ATYR89
ASER157
AALA158
AHIS276

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
ALEU66
AHOH514
ALYS50
AHIS57
ALEU58
AARG59

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 403
ChainResidue
AHIS57
AASN137
AASN171
AVAL172
AARG177
AEDO404
AHOH524

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
ALYS50
AASP56
AHIS57
AASN171
AEDO403
AHOH565

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 405
ChainResidue
AGLN78
ASER150
ASER150
AHOH501
AHOH501
AHOH502
AHOH502

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 406
ChainResidue
ATHR48
AGLU49
ATRP138
AASP141
AHOH522

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"HGGXW"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_03014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03014","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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