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1DOZ

CRYSTAL STRUCTURE OF FERROCHELATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004325molecular_functionferrochelatase activity
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006783biological_processheme biosynthetic process
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 900
ChainResidue
AHOH1202
AHOH1203
AHOH1204
AHOH1205
AHOH1206
AHOH1207

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
AHOH1211
AHOH1212
AHOH1213
AHOH1208
AHOH1209
AHOH1210

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AGLU20
AHOH1214
AHOH1215
AHOH1216
AHOH1217
AHOH1218

Functional Information from PROSITE/UniProt
site_idPS00534
Number of Residues19
DetailsFERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.EfGDp...Y
ChainResidueDetails
ALEU178-TYR196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H
ChainResidueDetails
ATYR13
AARG31
AHIS183
ALYS188

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751
ChainResidueDetails
AGLU20

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323
ChainResidueDetails
AARG30
ASER54
ATYR125

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:12761666
ChainResidueDetails
AARG46
AASP268
AGLU272

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000305|PubMed:12761666, ECO:0000305|PubMed:16140324, ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751
ChainResidueDetails
AGLU264

218853

PDB entries from 2024-04-24

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