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1CM5

CRYSTAL STRUCTURE OF C418A,C419A MUTANT 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
A0016746molecular_functionacyltransferase activity
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
B0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CO3 A 760
ChainResidue
AARG176
AALA418
APHE432
AARG435
ALEU604
AILE606
AHOH1065

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO3 B 760
ChainResidue
BPHE432
BARG435
BLEU604
BARG176
BALA418

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1056
ChainResidue
AALA652
ALEU654
AGLU700
AGLY701

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA B 1057
ChainResidue
BALA652
BLEU654
BGLU700
BGLY701

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
AALA419
BALA419

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Cysteine radical intermediate => ECO:0000269|PubMed:1310545
ChainResidueDetails
AVAL420
BVAL420

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALEU63
AMET117
AASP195
ALEU454
BLEU63
BMET117
BASP195
BLEU454

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
AARG107
AALA124
AGLY467
ALEU654
BARG107
BALA124
BGLY467
BLEU654

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ATYR541
ALEU591
BTYR541
BLEU591

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Glycine radical => ECO:0000269|PubMed:1310545
ChainResidueDetails
ATYR735
BTYR735

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 30
ChainResidueDetails
AALA334hydrogen bond donor, radical stabiliser
AALA419covalently attached, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, leaving group (radical), radical combinant
AVAL420hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, hydrogen radical relay
ATYR735hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 30
ChainResidueDetails
BALA334hydrogen bond donor, radical stabiliser
BALA419covalently attached, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, leaving group (radical), radical combinant
BVAL420hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, hydrogen radical relay
BTYR735hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor

222036

PDB entries from 2024-07-03

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