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1N0I

Crystal Structure of Ferrochelatase with Cadmium bound at active site

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 PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CD A 910
ChainResidue
ATYR13
AHIS183
ASER222
AGLU264
AHOH982
AHOH1052

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CD A 911
ChainResidue
AHOH962
AHOH1264
AHIS262
AHOH924
AHOH960

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 912
ChainResidue
AGLU145
ALYS307

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 913
ChainResidue
AARG33
APHE117
ASER146
AGLN199

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 900
ChainResidue
AHOH1266
AHOH1267
AHOH1268
AHOH1269
AHOH1270
AHOH1271

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
AHOH1272
AHOH1273
AHOH1274
AHOH1275
AHOH1276
AHOH1277

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 902
ChainResidue
AGLU20
AHOH1278
AHOH1279
AHOH1280
AHOH1281
AHOH1282

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hrk
ChainResidueDetails
AGLU264
AHIS262
AHIS183

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PDB entries from 2024-09-18

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