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3M4Z

Crystal Structure of B. subtilis ferrochelatase with Cobalt bound at the 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 CO A 310
ChainResidue
AHIS182
AGLU263
AHOH460
AHOH514
AHOH531
AHOH532

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 311
ChainResidue
AHOH511
AHOH512
AHOH513
AHOH424
AHOH509
AHOH510

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 312
ChainResidue
AHOH394
AHOH453
AHOH456
AHOH459
AHOH534
AHOH535

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 313
ChainResidue
AGLU19
AHOH536
AHOH537
AHOH538
AHOH539
AHOH540

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 314
ChainResidue
AARG32
ASER145
AGLN198
AHOH512

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 315
ChainResidue
AGLU144
ALYS306

Functional Information from PROSITE/UniProt
site_idPS00534
Number of Residues19
DetailsFERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.EfGDp...Y
ChainResidueDetails
ALEU177-TYR195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H
ChainResidueDetails
ATYR12
AARG30
AHIS182
ALYS187

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751
ChainResidueDetails
AGLU19

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323
ChainResidueDetails
AARG29
ASER53
ATYR124

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:12761666
ChainResidueDetails
AARG45
AASP267
AGLU271

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
AGLU263

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PDB entries from 2024-07-31

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