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2PFL

CRYSTAL STRUCTURE OF PFL FROM E.COLI

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_processglycolytic fermentation via PFL pathway
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_processglycolytic fermentation via PFL pathway
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1001
ChainResidue
BHOH2311

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 2001
ChainResidue
AALA652
ALEU654
AGLU700
AGLY701
AHOH2279

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 2002
ChainResidue
BGLY701
BALA652
BLEU654
BGLU700

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 Residues2
DetailsACT_SITE: S-acetylcysteine intermediate => ECO:0000269|PubMed:1310545
ChainResidueDetails
ACYS418
BCYS418

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000269|PubMed:1310545
ChainResidueDetails
ACYS419
BCYS419

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS62
ALYS116
ALYS194
ALYS453
BLYS62
BLYS116
BLYS194
BLYS453

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS106
ALYS123
ALYS466
ALYS653
BLYS106
BLYS123
BLYS466
BLYS653

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS540
ALYS590
BLYS540
BLYS590

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Glycine radical => ECO:0000269|PubMed:1310545
ChainResidueDetails
AGLY734
BGLY734

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10574800, 10648809, 10425676, 10504733
ChainResidueDetails
ACYS419
AGLY734
ATRP333
ACYS418

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10574800, 10648809, 10425676, 10504733
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 2025-07-02

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