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7S3V

Structure of HsKYNase_66, an evolved variant of human kynureninase with greatly increased activity towards kynurenine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006569biological_processtryptophan catabolic process
A0009435biological_processNAD biosynthetic process
A0016787molecular_functionhydrolase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0019441biological_processtryptophan catabolic process to kynurenine
A0019805biological_processquinolinate biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0030429molecular_functionkynureninase activity
A0034341biological_processresponse to type II interferon
A0034354biological_process'de novo' NAD biosynthetic process from tryptophan
A0034516biological_processresponse to vitamin B6
A0042803molecular_functionprotein homodimerization activity
A0043420biological_processanthranilate metabolic process
A0097053biological_processL-kynurenine catabolic process
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006569biological_processtryptophan catabolic process
B0009435biological_processNAD biosynthetic process
B0016787molecular_functionhydrolase activity
B0019363biological_processpyridine nucleotide biosynthetic process
B0019441biological_processtryptophan catabolic process to kynurenine
B0019805biological_processquinolinate biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0030429molecular_functionkynureninase activity
B0034341biological_processresponse to type II interferon
B0034354biological_process'de novo' NAD biosynthetic process from tryptophan
B0034516biological_processresponse to vitamin B6
B0042803molecular_functionprotein homodimerization activity
B0043420biological_processanthranilate metabolic process
B0097053biological_processL-kynurenine catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03017
ChainResidueDetails
ALEU137
ASER221
BLEU137
BSER221

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03017, ECO:0000269|PubMed:17300176
ChainResidueDetails
ATHR138
BTYR275
BTRP305
BTHR333
AASP250
AHIS253
ATYR275
ATRP305
ATHR333
BTHR138
BASP250
BHIS253

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
APHE165
BPHE165

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALLP276
BLLP276

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PDB entries from 2024-11-06

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