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

2QD4

Wild type human ferrochelatase crystallized with MnCl2

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 Residues5
DetailsBINDING SITE FOR RESIDUE CL A 701
ChainResidue
ATYR123
ASER130
AILE132
AHIS341
AILE342

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 924
ChainResidue
BHOH1031
BTYR623
BSER630
BHIS841
BILE842

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 703
ChainResidue
ALYS397
AGLN398
AHOH965
BTYR793

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 925
ChainResidue
AHOH869
BLYS897
BGLN898
BHOH1029

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 705
ChainResidue
ASER402
BARG827

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 706
ChainResidue
AARG327
BSER902

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 501
ChainResidue
ACYS196
AARG272
ASER402
ACYS403
ACYS406
ACYS411

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES B 502
ChainResidue
BCYS696
BARG772
BSER902
BCYS903
BCYS906
BCYS911

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CHD A 801
ChainResidue
ALEU92
APHE93
ALEU98
AARG115
ASER197
APRO266
AVAL269
AVAL305
ATRP310
ACHD802
AHOH978
AHOH979
AHOH1007

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CHD A 802
ChainResidue
AMET99
AARG114
AARG115
APRO266
AMET308
ACHD801
ACHD803
AHOH930

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD A 803
ChainResidue
APRO102
AARG114
ACHD802
AHOH942
BILE603

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CHD B 926
ChainResidue
BMET599
BLEU601
BILE611
BARG615
BPRO766
BSER768
BCHD927
BCHD928
BHOH1117

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CHD B 927
ChainResidue
AILE103
ALYS106
APHE110
BLEU601
BPRO602
BARG614
BCHD926
BHOH1118

site_idBC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE CHD B 928
ChainResidue
BLEU592
BPHE593
BLEU598
BARG615
BSER697
BHIS763
BLEU765
BPRO766
BVAL769
BVAL805
BTRP810
BCHD926
BHOH1128
BHOH1149

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
BHOH929
APRO277
ASER281
ATRP301
AHOH804
AHOH806
BPRO777
BSER781
BTRP801

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_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hrk
ChainResidueDetails
AGLU343
AHIS263
AHIS341

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1hrk
ChainResidueDetails
BHIS841
BHIS763
BGLU843

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

243911

PDB entries from 2025-10-29

PDB statisticsPDBj update infoContact PDBjnumon