Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4MK4

S197C variant of human ferrochelatase.

Replaces:  4F4G
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
ACYS403
ACYS406
ACYS411
AHOH616

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
ATRP301
AHOH679
BPRO277
BSER281
BTRP301
BHOH642
APRO277
AGLN278
ASER281

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CHD A 503
ChainResidue
ALEU92
ALEU98
AARG115
ALYS118
AILE119
ATHR198
AHIS263
AVAL305
ACHD504
AHOH608
AHOH613
AHOH663

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CHD A 504
ChainResidue
ALEU98
AMET99
AARG115
ASER268
AARG272
AVAL305
ACHD503

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FES B 501
ChainResidue
BCYS196
BARG272
BCYS403
BCYS406
BCYS411

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CHD B 502
ChainResidue
BPHE93
BLEU98
BMET99
BILE111
BARG114
BARG115
BCHD504

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CHD B 503
ChainResidue
BMET76
BPHE93
BLEU98
BARG115
BCYS197
BHIS263

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CHD B 504
ChainResidue
ALYS106
BARG114
BCHD502

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
BMET76
BLEU92
BLEU98
BARG164
BTYR165
BHIS263metal ligand, proton acceptor
BASP340
BGLU343metal ligand, proton acceptor
BGLU347

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon