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1KYQ

Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0003824molecular_functioncatalytic activity
A0004325molecular_functionferrochelatase activity
A0005515molecular_functionprotein binding
A0005575cellular_componentcellular_component
A0006779biological_processporphyrin-containing compound biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0019354biological_processsiroheme biosynthetic process
A0043115molecular_functionprecorrin-2 dehydrogenase activity
A0051266molecular_functionsirohydrochlorin ferrochelatase activity
B0000103biological_processsulfate assimilation
B0003824molecular_functioncatalytic activity
B0004325molecular_functionferrochelatase activity
B0005515molecular_functionprotein binding
B0005575cellular_componentcellular_component
B0006779biological_processporphyrin-containing compound biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016829molecular_functionlyase activity
B0019354biological_processsiroheme biosynthetic process
B0043115molecular_functionprecorrin-2 dehydrogenase activity
B0051266molecular_functionsirohydrochlorin ferrochelatase activity
C0000103biological_processsulfate assimilation
C0003824molecular_functioncatalytic activity
C0004325molecular_functionferrochelatase activity
C0005515molecular_functionprotein binding
C0005575cellular_componentcellular_component
C0006779biological_processporphyrin-containing compound biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016829molecular_functionlyase activity
C0019354biological_processsiroheme biosynthetic process
C0043115molecular_functionprecorrin-2 dehydrogenase activity
C0051266molecular_functionsirohydrochlorin ferrochelatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE NAD A 800
ChainResidue
AGLY20
AASP92
APHE93
AILE114
APRO115
AHOH811
AHOH839
AHOH904
AHOH915
AGLY21
AGLY22
AGLU23
AVAL24
AVAL42
ASER43
APRO44
AASP45

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD B 801
ChainResidue
BILE19
BGLY20
BGLY21
BGLY22
BGLU23
BVAL24
BVAL42
BSER43
BPRO44
BASP45
BASP92
BPHE93
BCYS113
BILE114
BPRO115
BALA140
BASP141
BHOH803
BHOH808
BHOH809
BHOH822
BHOH847
BHOH883
BHOH968
BHOH986
BHOH991
BHOH1017

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD C 802
ChainResidue
CILE19
CGLY20
CGLY21
CGLY22
CGLU23
CVAL24
CVAL42
CSER43
CPRO44
CASP45
CASP92
CPHE93
CCYS113
CILE114
CALA140
CASP141
CHOH809
CHOH811
CHOH812
CHOH877
CHOH925

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11980703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11980703, 12196147
ChainResidueDetails
AASP141

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11980703, 12196147
ChainResidueDetails
BASP141

site_idCSA3
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11980703, 12196147
ChainResidueDetails
CASP141

site_idMCSA1
Number of Residues1
DetailsM-CSA 610
ChainResidueDetails
AASN153proton acceptor, proton donor

site_idMCSA2
Number of Residues1
DetailsM-CSA 610
ChainResidueDetails
BASN153proton acceptor, proton donor

site_idMCSA3
Number of Residues1
DetailsM-CSA 610
ChainResidueDetails
CASN153proton acceptor, proton donor

250059

PDB entries from 2026-03-04

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