1BMT
HOW A PROTEIN BINDS B12: A 3.O ANGSTROM X-RAY STRUCTURE OF THE B12-BINDING DOMAINS OF METHIONINE SYNTHASE
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE COB A 122 |
| Chain | Residue |
| A | GLU694 |
| A | HIS759 |
| A | ASP760 |
| A | ILE761 |
| A | GLY762 |
| A | ILE765 |
| A | GLY802 |
| A | LEU803 |
| A | SER804 |
| A | LEU806 |
| A | ILE807 |
| A | MET698 |
| A | THR808 |
| A | LEU831 |
| A | GLY834 |
| A | ALA835 |
| A | VAL857 |
| A | GLN858 |
| A | ASN859 |
| A | ALA860 |
| A | THR863 |
| B | GLN677 |
| A | MET701 |
| B | GLU680 |
| B | ARG683 |
| B | TYR731 |
| B | PHE735 |
| A | GLY705 |
| A | LEU715 |
| A | VAL718 |
| A | GLY756 |
| A | ASP757 |
| A | VAL758 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE COB B 122 |
| Chain | Residue |
| A | ALA738 |
| A | GLU741 |
| B | GLU694 |
| B | MET698 |
| B | MET701 |
| B | VAL704 |
| B | GLY705 |
| B | LEU715 |
| B | VAL718 |
| B | MET725 |
| B | ILE751 |
| B | GLY756 |
| B | ASP757 |
| B | VAL758 |
| B | HIS759 |
| B | ASP760 |
| B | ILE761 |
| B | GLY762 |
| B | ILE765 |
| B | GLY802 |
| B | LEU803 |
| B | SER804 |
| B | LEU806 |
| B | ILE807 |
| B | THR808 |
| B | GLY834 |
| B | ALA835 |
| B | GLN858 |
| B | ASN859 |
| B | ALA860 |
| B | THR863 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 270 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7992050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"7992050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BMT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 7712296, 7992050, 11731805 |
| Chain | Residue | Details |
| A | SER810 | |
| A | ASP757 | |
| A | HIS759 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 7712296, 7992050, 11731805 |
| Chain | Residue | Details |
| B | SER810 | |
| B | ASP757 | |
| B | HIS759 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 268 |
| Chain | Residue | Details |
| A | ASP757 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS759 | hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, increase nucleophilicity, metal ligand, proton acceptor, proton donor |
| A | SER810 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 268 |
| Chain | Residue | Details |
| B | ASP757 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS759 | hydrogen bond acceptor, hydrogen bond donor, increase electrophilicity, increase nucleophilicity, metal ligand, proton acceptor, proton donor |
| B | SER810 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
