Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1HRK

CRYSTAL STRUCTURE 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 Residues15
DetailsBINDING SITE FOR RESIDUE CHD A 1501
ChainResidue
ALEU92
AHOH1544
AHOH1559
AHOH1569
AHOH1595
AHOH1633
AHOH1763
ALEU98
ASER197
AHIS263
ALEU265
APRO266
AVAL269
ATRP310
ACHD1502

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CHD A 1502
ChainResidue
AMET99
AARG114
ALEU115
APRO266
AMET308
ACHD1501
ACHD1503
AHOH1622
AHOH1679
AHOH1685
AHOH1698
AHOH1713
AHOH1726

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD A 1503
ChainResidue
ALEU107
ACHD1502
AHOH1698
AHOH1726
BPHE110

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE CHD B 2501
ChainResidue
BLEU92
BPHE93
BLEU98
BSER197
BHIS263
BLEU265
BPRO266
BVAL269
BTRP310
BCHD2502
BHOH3079
BHOH3091
BHOH3092
BHOH3094
BHOH3112
BHOH3218
BHOH3281

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CHD B 2502
ChainResidue
BMET99
BARG114
BLEU115
BPRO266
BMET308
BCHD2501
BCHD2503
BHOH3157
BHOH3173
BHOH3214
BHOH3219
BHOH3264

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CHD B 2503
ChainResidue
ALYS106
APHE110
BLEU101
BARG114
BCHD2502
BHOH3173
BHOH3219
BHOH3298

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 1499
ChainResidue
ACYS196
AARG272
ASER402
ACYS403
ACYS406
ACYS411

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES B 2999
ChainResidue
BCYS196
BARG272
BSER402
BCYS403
BCYS406
BCYS411

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
BHIS230
BASP383

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ACYS196
ACYS403
ACYS406
ACYS411
BCYS196
BCYS403
BCYS406
BCYS411

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P22315
ChainResidueDetails
ALYS138
BLYS138

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P22315
ChainResidueDetails
ALYS415
BLYS415

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 11175906, 11502175, 1175906
ChainResidueDetails
AHIS263
AGLU343
AGLU347
AASP340
AARG164
ATYR165

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon