Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WM1

The crystal structure of human alpha-amino-beta-carboxymuconate- epsilon-semialdehyde decarboxylase in complex with 1,3- dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis

Functional Information from GO Data
ChainGOidnamespacecontents
A0001760molecular_functionaminocarboxymuconate-semialdehyde decarboxylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006569biological_processtryptophan catabolic process
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0016831molecular_functioncarboxy-lyase activity
A0019748biological_processsecondary metabolic process
A0046872molecular_functionmetal ion binding
A1901360biological_processorganic cyclic compound metabolic process
A1904985biological_processnegative regulation of quinolinate biosynthetic process
A1905004biological_processpicolinic acid biosynthetic process
A1905012biological_processregulation of 'de novo' NAD biosynthetic process from tryptophan
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1333
ChainResidue
AHIS6
AHIS8
AHIS174
AASP291
AHOH2215

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 13P A 1334
ChainResidue
AASP291
APHE294
ALEU296
AHOH2127
AHOH2215
AHOH2216
AARG47
APRO77
AHIS174
ATRP191

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1335
ChainResidue
AVAL147
AASN148
AGLU149
AHOH2095

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19843166
ChainResidueDetails
AHIS6
AHIS8
AHIS174
AASP291

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:19843166
ChainResidueDetails
AARG47

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon