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4EXQ

CRYSTAL STRUCTURE of UROPORPHYRINOGEN DECARBOXYLASE (UPD) FROM BURKHOLDERIA THAILANDENSIS E264

Functional Information from GO Data
ChainGOidnamespacecontents
A0004853molecular_functionuroporphyrinogen decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006778biological_processporphyrin-containing compound metabolic process
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0006783biological_processheme biosynthetic process
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0019353biological_processprotoporphyrinogen IX biosynthetic process from glutamate
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 401
ChainResidue
ATHR9
ATHR19
AASP20
APRO307

Functional Information from PROSITE/UniProt
site_idPS00906
Number of Residues10
DetailsUROD_1 Uroporphyrinogen decarboxylase signature 1. PIWLMRQAGR
ChainResidueDetails
APRO23-ARG32

site_idPS00907
Number of Residues17
DetailsUROD_2 Uroporphyrinogen decarboxylase signature 2. IGFSGsPWTLacYmv.EG
ChainResidueDetails
AILE148-GLY164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00218","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00218","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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