1CM5
CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0008861 | molecular_function | formate C-acetyltransferase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0044814 | biological_process | glycolytic fermentation via PFL pathway |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0008861 | molecular_function | formate C-acetyltransferase activity |
| B | 0016020 | cellular_component | membrane |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0044814 | biological_process | glycolytic fermentation via PFL pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 A 760 |
| Chain | Residue |
| A | ARG176 |
| A | ALA418 |
| A | PHE432 |
| A | ARG435 |
| A | LEU604 |
| A | ILE606 |
| A | HOH1065 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO3 B 760 |
| Chain | Residue |
| B | PHE432 |
| B | ARG435 |
| B | LEU604 |
| B | ARG176 |
| B | ALA418 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 1056 |
| Chain | Residue |
| A | ALA652 |
| A | LEU654 |
| A | GLU700 |
| A | GLY701 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1057 |
| Chain | Residue |
| B | ALA652 |
| B | LEU654 |
| B | GLU700 |
| B | GLY701 |
Functional Information from PROSITE/UniProt
| site_id | PS00850 |
| Number of Residues | 9 |
| Details | GLY_RADICAL_1 Glycine radical domain signature. TiRVSGYAV |
| Chain | Residue | Details |
| A | THR729-VAL737 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1244 |
| Details | Domain: {"description":"PFL","evidences":[{"source":"PROSITE-ProRule","id":"PRU00887","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 256 |
| Details | Domain: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"S-acetylcysteine intermediate","evidences":[{"source":"PubMed","id":"1310545","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine radical intermediate","evidences":[{"source":"PubMed","id":"1310545","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Glycine radical","evidences":[{"source":"PubMed","id":"1310545","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 30 |
| Chain | Residue | Details |
| A | TRP333 | hydrogen bond donor, radical stabiliser |
| A | ALA418 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, leaving group (radical), radical combinant |
| A | ALA419 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, hydrogen radical relay |
| A | GLY734 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 30 |
| Chain | Residue | Details |
| B | TRP333 | hydrogen bond donor, radical stabiliser |
| B | ALA418 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, leaving group (radical), radical combinant |
| B | ALA419 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, hydrogen radical relay |
| B | GLY734 | hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor |
