Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| A | 0008817 | molecular_function | corrinoid adenosyltransferase activity |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
| B | 0008817 | molecular_function | corrinoid adenosyltransferase activity |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 998 |
| Chain | Residue |
| A | THR42 |
| A | GLU128 |
| A | ATP999 |
| A | HOH1331 |
| A | HOH1332 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1001 |
| Chain | Residue |
| B | HOH1381 |
| B | THR242 |
| B | GLU328 |
| B | ATP1000 |
| B | HOH1380 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE B12 A 800 |
| Chain | Residue |
| A | LYS66 |
| A | TRP93 |
| A | TYR131 |
| A | ARG161 |
| A | ATP999 |
| A | HOH1239 |
| B | ARG216 |
| B | PRO279 |
| B | HIS280 |
| B | GLN296 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP A 999 |
| Chain | Residue |
| A | ASN37 |
| A | GLY38 |
| A | LYS39 |
| A | GLY40 |
| A | LYS41 |
| A | THR42 |
| A | THR43 |
| A | GLU128 |
| A | ARG161 |
| A | HIS182 |
| A | ASP195 |
| A | B12800 |
| A | MG998 |
| A | HOH1247 |
| A | HOH1331 |
| A | HOH1332 |
| A | HOH1421 |
| B | ARG251 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP B 1000 |
| Chain | Residue |
| A | ARG51 |
| B | ASN237 |
| B | GLY238 |
| B | LYS239 |
| B | GLY240 |
| B | LYS241 |
| B | THR242 |
| B | THR243 |
| B | GLU328 |
| B | TYR331 |
| B | HIS382 |
| B | ASP395 |
| B | MG1001 |
| B | HOH1214 |
| B | HOH1367 |
| B | HOH1380 |
| B | HOH1381 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11148030 |
| Chain | Residue | Details |
| A | THR43 | |
| A | LYS41 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11148030 |
| Chain | Residue | Details |
| B | THR243 | |
| B | LYS241 | |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 853 |
| Chain | Residue | Details |
| A | ASN37 | electrostatic stabiliser |
| A | LYS39 | electrostatic stabiliser |
| A | LYS41 | electrostatic stabiliser |
| A | THR42 | electrostatic stabiliser, metal ligand |
| A | THR43 | electrostatic stabiliser |
| A | ARG51 | electrostatic stabiliser |
| A | PHE91 | electrostatic stabiliser |
| A | TRP93 | electrostatic stabiliser |
| A | GLU128 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 853 |
| Chain | Residue | Details |
| B | ASN237 | electrostatic stabiliser |
| B | LYS239 | electrostatic stabiliser |
| B | LYS241 | electrostatic stabiliser |
| B | THR242 | electrostatic stabiliser, metal ligand |
| B | THR243 | electrostatic stabiliser |
| B | ARG251 | electrostatic stabiliser |
| B | PHE291 | electrostatic stabiliser |
| B | TRP293 | electrostatic stabiliser |
| B | GLU328 | metal ligand |