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4KLC

E343D/F110A Double mutant of human ferrochelatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004325molecular_functionferrochelatase activity
A0006783biological_processheme biosynthetic process
B0004325molecular_functionferrochelatase activity
B0006783biological_processheme biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES A 501
ChainResidue
ACYS196
AARG272
ASER402
ACYS403
ACYS406
ACYS411
AHOH762

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 502
ChainResidue
APRO79
ALEU92
APHE93
ALEU98
ATYR123
ASER197
ATHR198
AHIS263
ALEU265
APRO266
ATRP310
APHE337
AHIS341
AILE342
AASP343
AGLY77
AGLY78

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES B 501
ChainResidue
BCYS196
BARG272
BSER402
BCYS403
BCYS406
BCYS411

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
APRO277
ASER281
AHOH693
BPRO277
BGLN278
BSER281
BLEU299
BTRP301

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM B 503
ChainResidue
BPHE88
BLEU98
BARG115
BILE119
BTYR123
BSER197
BTHR198
BHIS263
BLEU265
BPRO266
BTYR276
BVAL305
BPHE337
BHIS341
BILE342

Functional Information from PROSITE/UniProt
site_idPS00534
Number of Residues19
DetailsFERROCHELATASE Ferrochelatase signature. ILfSaHSLPmsvv.NrGDp...Y
ChainResidueDetails
AILE258-TYR276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17261801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HRE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17261801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HRK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HRC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HRK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P22315","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P22315","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 578
ChainResidueDetails
AMET76
ALEU92
ALEU98
AARG164
ATYR165
AHIS263metal ligand, proton acceptor
AASP340
AASP343metal ligand, proton acceptor
AGLU347

site_idMCSA2
Number of Residues9
DetailsM-CSA 578
ChainResidueDetails
BMET76
BLEU92
BLEU98
BARG164
BTYR165
BHIS263metal ligand, proton acceptor
BASP340
BASP343metal ligand, proton acceptor
BGLU347

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PDB entries from 2025-08-06

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