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1QZ9

The Three Dimensional Structure of Kynureninase from Pseudomonas fluorescens

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006569biological_processtryptophan catabolic process
A0009435biological_processNAD biosynthetic process
A0016787molecular_functionhydrolase activity
A0019363biological_processpyridine nucleotide biosynthetic process
A0019805biological_processquinolinate biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0030429molecular_functionkynureninase activity
A0034354biological_process'de novo' NAD biosynthetic process from tryptophan
A0043420biological_processanthranilate metabolic process
A0061981molecular_function3-hydroxykynureninase activity
A0097053biological_processL-kynurenine catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AHIS204
AARG375
AHOH1353

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP A 1227
ChainResidue
ATHR172
AASP201
AALA203
AHIS204
ACYS224
ATYR226
ALYS227
ATRP256
AGLY281
ATHR282
AHOH1256
ATHR96
ATHR97
ASER98
APHE129
ATHR131
AASP132

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE P3G A 701
ChainResidue
ATRP256
AHIS259
AARG261
AMET265
AARG369
AHOH1636

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01970, ECO:0000269|PubMed:14756555
ChainResidueDetails
ATHR97
ASER98
ATHR172
AASP201
AHIS204

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
APHE129

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:14756555
ChainResidueDetails
ATYR226
ATRP256
ATHR282

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS227

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 14756555
ChainResidueDetails
AASP201
APHE129
ALYS227

site_idMCSA1
Number of Residues5
DetailsM-CSA 742
ChainResidueDetails
APHE129electrostatic stabiliser
AASP201electrostatic stabiliser
ATYR226hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
ALYS227electron pair acceptor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG375electrostatic stabiliser

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PDB entries from 2024-07-10

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