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6PR1

R260A/S128A S. typhimurium siroheme synthase

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0016829molecular_functionlyase activity
A0019354biological_processsiroheme biosynthetic process
A0032259biological_processmethylation
A0043115molecular_functionprecorrin-2 dehydrogenase activity
A0051266molecular_functionsirohydrochlorin ferrochelatase activity
A0051287molecular_functionNAD binding
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
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 Residues4
Detailsbinding site for residue CL A 601
ChainResidue
AALA128
AGLY130
ASER132
APRO133

site_idAC2
Number of Residues22
Detailsbinding site for residue SAH A 602
ChainResidue
AILE306
APHE307
ATHR331
AALA332
ACYS336
ATYR381
AMET382
AVAL408
AASN410
AGLY411
APRO436
AALA437
ALEU438
AHOH763
AHOH799
AHOH800
AHOH857
APRO225
ALEU250
AGLY301
AGLY302
AASP303

site_idAC3
Number of Residues5
Detailsbinding site for residue CL B 601
ChainResidue
BALA128
BGLY130
BTHR131
BSER132
BPRO133

site_idAC4
Number of Residues21
Detailsbinding site for residue SAH B 602
ChainResidue
BPRO225
BGLY301
BGLY302
BASP303
BILE306
BPHE307
BTHR331
BALA332
BCYS336
BTYR381
BMET382
BVAL408
BASN410
BGLY411
BPRO436
BALA437
BLEU438
BHOH750
BHOH847
BHOH852
BHOH862

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_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:14595395
ChainResidueDetails
AASP248
BASP248

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:14595395
ChainResidueDetails
ALYS270
BLYS270

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:14595395
ChainResidueDetails
AASP22
BASP22
BLEU43
BPRO225
BGLY301
BILE306
BTHR331
BMET382
BGLY411
BALA437
ALEU43
APRO225
AGLY301
AILE306
ATHR331
AMET382
AGLY411
AALA437

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:14595395
ChainResidueDetails
AALA128
BALA128

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

221371

PDB entries from 2024-06-19

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