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6RWV

Structure of apo-LmCpfC

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 Residues9
Detailsbinding site for residue GOL A 401
ChainResidue
ATYR16
AALA56
ATHR59
AGLU60
AILE83
ALEU85
APRO90
AHOH504
AHOH556

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
ATYR12
AHIS182
AHIS261
AGLU263
APO4409
AHOH502
AHOH665

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
ATYR64
AILE83
AALA95

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 404
ChainResidue
AASP18
AILE21
AARG43
AHIS47
AGLY51
ALEU52

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 405
ChainResidue
ATYR12
ASER120
APO4408
AHOH566

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 406
ChainResidue
AILE28
AHIS30
AASP75
ATHR225
APO4408
AHOH505

site_idAC7
Number of Residues4
Detailsbinding site for residue GOL A 407
ChainResidue
ALYS33
ASER35
AASN71
AHOH501

site_idAC8
Number of Residues7
Detailsbinding site for residue PO4 A 408
ChainResidue
ATYR12
AILE28
ALYS86
AHIS87
AGOL405
AGOL406
AHOH561

site_idAC9
Number of Residues7
Detailsbinding site for residue PO4 A 409
ChainResidue
ATYR12
AHIS182
AGLU263
AGOL402
AHOH505
AHOH517
AHOH525

site_idAD1
Number of Residues2
Detailsbinding site for residue K A 410
ChainResidue
AGLU186
AGLY231

site_idAD2
Number of Residues1
Detailsbinding site for residue K A 411
ChainResidue
AGLU122

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 site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00323","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31794133","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SV3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00323","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31794133","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SV3","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00323","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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