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

6P5X

Sirohydrochlorin-bound S. typhimurium siroheme synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004325molecular_functionferrochelatase activity
A0004851molecular_functionuroporphyrin-III C-methyltransferase activity
A0006779biological_processporphyrin-containing compound biosynthetic process
A0008168molecular_functionmethyltransferase activity
A0009236biological_processcobalamin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0019354biological_processsiroheme biosynthetic process
A0032259biological_processmethylation
A0043115molecular_functionprecorrin-2 dehydrogenase activity
A0051266molecular_functionsirohydrochlorin ferrochelatase activity
A0051287molecular_functionNAD binding
B0003824molecular_functioncatalytic activity
B0004325molecular_functionferrochelatase activity
B0004851molecular_functionuroporphyrin-III C-methyltransferase activity
B0006779biological_processporphyrin-containing compound biosynthetic process
B0008168molecular_functionmethyltransferase activity
B0009236biological_processcobalamin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016829molecular_functionlyase activity
B0019354biological_processsiroheme biosynthetic process
B0032259biological_processmethylation
B0043115molecular_functionprecorrin-2 dehydrogenase activity
B0051266molecular_functionsirohydrochlorin ferrochelatase activity
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue SAH A 501
ChainResidue
APRO225
ATYR381
AMET382
AVAL408
AGLY411
APRO436
AALA437
ALEU438
AHOH634
AHOH652
AHOH694
AGLY301
AHOH712
AGLY302
AASP303
AILE306
APHE307
ATHR331
AALA332
ACYS336

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 502
ChainResidue
APHE307
AARG309
BTHR345

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 503
ChainResidue
AGLN400
AMET403
AHOH697
AHOH704

site_idAC4
Number of Residues20
Detailsbinding site for residue SAH B 501
ChainResidue
BPRO225
BGLY301
BGLY302
BASP303
BILE306
BPHE307
BTHR331
BALA332
BCYS336
BTYR381
BMET382
BVAL408
BASN410
BGLY411
BPRO436
BALA437
BLEU438
BHOH635
BHOH697
BHOH706

site_idAC5
Number of Residues36
Detailsbinding site for residue SHN B 502
ChainResidue
AARG162
ALYS166
AARG175
AARG176
ATRP179
AARG260
AARG261
AASP262
BLYS27
BASN101
BASP104
BALA105
BILE112
BMET113
BSER115
BSER127
BALA128
BGLY129
BGLY130
BTHR131
BSER132
BPRO133
BVAL134
BARG137
BARG140
BHOH604
BHOH607
BHOH612
BHOH624
BHOH628
BHOH629
BHOH637
BHOH652
BHOH678
BHOH679
BHOH688

Functional Information from PROSITE/UniProt
site_idPS00839
Number of Residues15
DetailsSUMT_1 Uroporphyrin-III C-methyltransferase signature 1. VGAGPGdagLLTLKG
ChainResidueDetails
AVAL221-GLY235

site_idPS00840
Number of Residues34
DetailsSUMT_2 Uroporphyrin-III C-methyltransferase signature 2. VvrLkgGDpfiFGrggeeletLchagipFsVvPG
ChainResidueDetails
AVAL296-GLY329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"14595395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues396
DetailsRegion: {"description":"Precorrin-2 dehydrogenase /sirohydrochlorin ferrochelatase"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 702
ChainResidueDetails
AASP248electrostatic stabiliser, proton acceptor, proton donor
ALYS270electrostatic stabiliser
AMET382electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 702
ChainResidueDetails
BASP248electrostatic stabiliser, proton acceptor, proton donor
BLYS270electrostatic stabiliser
BMET382electrostatic stabiliser

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon