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1MZO

Crystal structure of pyruvate formate-lyase with pyruvate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006006biological_processglucose metabolic process
A0008861molecular_functionformate C-acetyltransferase activity
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0044814biological_processpyruvate fermentation via PFL
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006006biological_processglucose metabolic process
B0008861molecular_functionformate C-acetyltransferase activity
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0044814biological_processpyruvate fermentation via PFL
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 1001
ChainResidue
AALA238
ALYS239
ATYR240
AGLY241
AGLY241

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR A 2001
ChainResidue
APHE432
AARG435
ALEU604
AILE606
AHOH2010
AARG176
AALA273
APHE327
ACYS418

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR B 2002
ChainResidue
BARG176
BALA272
BALA273
BCYS418
BPHE432
BARG435
BLEU604
BILE606
BHOH2012

Functional Information from PROSITE/UniProt
site_idPS00850
Number of Residues9
DetailsGLY_RADICAL_1 Glycine radical domain signature. TiRVSGYAV
ChainResidueDetails
ATHR729-VAL737

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsDomain: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"S-acetylcysteine intermediate","evidences":[{"source":"PubMed","id":"1310545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Cysteine radical intermediate","evidences":[{"source":"PubMed","id":"1310545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Glycine radical","evidences":[{"source":"PubMed","id":"1310545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 2pfl
ChainResidueDetails
ACYS419
AGLY734
ATRP333
ACYS418

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 2pfl
ChainResidueDetails
BCYS419
BGLY734
BTRP333
BCYS418

site_idMCSA1
Number of Residues4
DetailsM-CSA 30
ChainResidueDetails
ATRP333hydrogen bond donor, radical stabiliser
ACYS418covalently attached, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, leaving group (radical), radical combinant
ACYS419hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, hydrogen radical relay
AGLY734hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 30
ChainResidueDetails
BTRP333hydrogen bond donor, radical stabiliser
BCYS418covalently attached, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, leaving group (radical), radical combinant
BCYS419hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, hydrogen radical relay
BGLY734hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor

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PDB entries from 2025-12-03

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