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2PNJ

Crystal structure of human ferrochelatase mutant with Phe 337 replaced by Ala

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 499
ChainResidue
ACYS196
ASER402
ACYS403
ACYS406
ACYS411

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CHD A 501
ChainResidue
AHIS263
AVAL269
AVAL305
ATRP310
ACHD502
AHOH556
AHOH590
ALEU92
APHE93
ALEU98
ASER197

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CHD A 502
ChainResidue
AMET99
AMET308
ATRP310
ACHD501
ACHD503
AHOH591

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CHD A 503
ChainResidue
ACHD502
BLEU107
BPHE110

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FES B 499
ChainResidue
BCYS196
BARG272
BCYS403
BCYS406
BCYS411

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CHD B 501
ChainResidue
BLEU92
BLEU98
BSER197
BHIS263
BVAL269
BTRP310
BHOH553
BHOH620

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD B 502
ChainResidue
BMET99
BARG114
BMET308
BCHD503
BHOH568

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CHD B 503
ChainResidue
AILE103
ALEU107
APHE110
BLEU107
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_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
BGLU343
BHIS263
BHIS341

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

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PDB entries from 2025-08-27

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