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8AT8

Structure of coproporphyrin III-LmCpfC

Functional Information from GO Data
ChainGOidnamespacecontents
A0004325molecular_functionferrochelatase activity
A0005737cellular_componentcytoplasm
A0006783biological_processheme biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DTVLIVSAHSL
ChainResidueDetails
AASP174-LEU184

site_idPS00534
Number of Residues19
DetailsFERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.QhNDp...Y
ChainResidueDetails
ALEU177-TYR195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3
ChainResidueDetails
ATYR12

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:31794133, ECO:0007744|PDB:6SV3
ChainResidueDetails
ATHR14
AARG29
AARG45
ASER53
ATYR124

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323
ChainResidueDetails
AHIS182
AGLU263

219869

PDB entries from 2024-05-15

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