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2QD5

Structure of wild type human ferrochelatase in complex with a lead-porphyrin compound

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 Residues3
DetailsBINDING SITE FOR RESIDUE PB A 1101
ChainResidue
AACY801
AACY803
APP9901

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PB B 1102
ChainResidue
BOXY1001
BPP91105
BACY1106

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FES A 501
ChainResidue
ACYS406
ACYS411
ACYS196
ASER402
ACYS403

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FES B 502
ChainResidue
BCYS696
BSER902
BCYS903
BCYS906
BCYS911

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CHD A 701
ChainResidue
AMET99
AARG115
APRO266
ASER268
AVAL305
AGLY306
AMET308
ACHD702
AHOH1176

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD A 702
ChainResidue
AARG114
ACHD701
BILE603
BLYS606
BPHE610

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CHD B 1103
ChainResidue
BLEU601
BPRO766
BSER768
BVAL805
BGLY806
BMET808
BCHD1104
BPP91105
BHOH1108
BHOH1162

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD B 1104
ChainResidue
ALYS106
APHE110
BLEU601
BPRO602
BCHD1103

site_idAC9
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PP9 A 901
ChainResidue
AMET76
APHE93
ALEU98
AARG115
AILE119
ASER195
ASER197
AHIS263
ALEU265
APRO266
AALA336
APHE337
AHIS341
AILE342
AACY801
AACY803
APB1101
AHOH1102
AHOH1160

site_idBC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE PP9 B 1105
ChainResidue
BMET576
BPHE593
BLEU598
BARG615
BTYR623
BTYR691
BSER697
BHIS763
BLEU765
BPRO766
BTYR776
BVAL805
BALA836
BPHE837
BHIS841
BILE842
BPB1102
BCHD1103
BACY1106
BHOH1154
BHOH1159

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE OXY B 1001
ChainResidue
BPB1102

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
APRO277
ASER281
ATRP301
AHOH1131
BPRO777
BSER781
BTRP801

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 801
ChainResidue
APP9901
APB1101
AMET76
ALEU98
ATYR165
ATYR191
ASER197
ATHR198

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY B 1106
ChainResidue
BHIS763
BSER764
BGLN802
BSER803
BLYS804
BTRP810
BPB1102
BPP91105

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 803
ChainResidue
ASER264
ASER303
ALYS304
ATRP310
APP9901
APB1101

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_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

218853

PDB entries from 2024-04-24

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