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3AQI

H240A variant 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 Residues6
DetailsBINDING SITE FOR RESIDUE FES A 501
ChainResidue
ACYS196
AARG272
ASER402
ACYS403
ACYS406
ACYS411

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CHD A 1
ChainResidue
ASER197
AHIS263
AVAL269
ATRP310
AHOH499
AHOH503
AHOH512
AHOH551
AHOH557
AHOH578
AHOH691
ACHD2
ALEU92
ALEU98

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CHD A 2
ChainResidue
ACHD1
ACHD3
AMET99
AARG114
AHOH518
AHOH567
AHOH602
AHOH701

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CHD A 3
ChainResidue
ACHD2
AHOH651
BLYS606
BPHE610

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 424
ChainResidue
AGLU80
AGLY127
AGLY129
ASER130
AHOH473
AHOH873

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES B 501
ChainResidue
BCYS696
BARG772
BSER902
BCYS903
BCYS906
BCYS911

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CHD B 4
ChainResidue
BCHD5
BCHD6
BHOH429
BHOH442
BHOH514
BHOH517
BMET599
BARG614
BPRO766

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD B 5
ChainResidue
ALYS106
APHE110
BCHD4
BHOH517
BHOH1023

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CHD B 6
ChainResidue
BCHD4
BHOH156
BHOH174
BHOH186
BHOH293
BHOH346
BHOH404
BHOH464
BMET576
BLEU592
BPHE593
BLEU598
BSER697
BHIS763
BPRO766
BVAL769
BTRP810

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
AGLU343metal ligand, proton acceptor
AGLU347

site_idMCSA2
Number of Residues9
DetailsM-CSA 578
ChainResidueDetails
BMET576
BLEU592
BLEU598
BARG664
BTYR665
BHIS763metal ligand, proton acceptor
BASP840
BGLU843metal ligand, proton acceptor
BGLU847

247947

PDB entries from 2026-01-21

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