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3HCO

Human ferrochelatase with Cd and protoporphyrin IX bound

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 FES A 501
ChainResidue
ACYS196
ASER402
ACYS403
ACYS406
ACYS411

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 1
ChainResidue
AHOH519
AHOH520
BHOH126
BPRO777
BGLN778
BSER781
BTRP801
APRO277
AGLN278
ASER281
ATRP301

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 424
ChainResidue
ASER264
ASER303
ATRP310
AHEM426

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BCT A 425
ChainResidue
ALEU98
ATYR165
ASER197
AHEM426
AHOH445

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CHD A 3
ChainResidue
ALEU101
APRO102
ALEU107
AARG114
BLYS606
BPHE610

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CHD A 4
ChainResidue
AMET99
ATHR100
ALEU101
AARG115
APRO266
ASER268
AVAL305
AGLY306
AMET308
AHEM426
AHOH467
AHOH560

site_idAC7
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 426
ChainResidue
ACHD4
AMET76
ALEU92
APHE93
ALEU98
AARG115
ATYR123
ASER197
ATHR198
AHIS263
APRO266
AVAL305
ATRP310
AALA336
AHIS341
AILE342
AIMD424
ABCT425
AHOH430
AHOH443
AHOH495
AHOH497

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES B 501
ChainResidue
BCYS696
BARG772
BSER902
BCYS903
BCYS906
BCYS911

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD B 2
ChainResidue
BHIS763
BSER764
BSER803
BTRP810
BHEM926

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD B 3
ChainResidue
BMET576
BLEU598
BTYR665
BHEM926

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD B 1
ChainResidue
ALYS106
ALEU107
APHE110
BPHE610
BCHD924

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CHD B 924
ChainResidue
BCHD1
BHOH195
BHOH304
BHOH361
BHOH362
BLEU601
BARG614
BARG615
BPRO766
BSER768
BVAL805
BGLY806
BHEM926

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 925
ChainResidue
BGLY806
BARG615

site_idBC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM B 926
ChainResidue
BIMD2
BIMD3
BHOH167
BHOH177
BHOH240
BHOH282
BMET576
BPHE593
BLEU598
BARG615
BTYR623
BSER697
BTHR698
BHIS763
BLEU765
BPRO766
BVAL805
BALA836
BPHE837
BHIS841
BILE842
BCHD924

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
DetailsACT_SITE:
ChainResidueDetails
AHIS230
AASP383
BHIS730
BASP883

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ACYS196
ACYS403
ACYS406
ACYS411
BCYS696
BCYS903
BCYS906
BCYS911

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P22315
ChainResidueDetails
ALYS138
BLYS638

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P22315
ChainResidueDetails
ALYS415
BLYS915

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

223532

PDB entries from 2024-08-07

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