1C9K
THE THREE DIMENSIONAL STRUCTURE OF ADENOSYLCOBINAMIDE KINASE/ ADENOSYLCOBINAMIDE PHOSPHATE GUALYLYLTRANSFERASE (COBU) COMPLEXED WITH GMP: EVIDENCE FOR A SUBSTRATE INDUCED TRANSFERASE ACTIVE SITE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0008820 | molecular_function | cobinamide phosphate guanylyltransferase activity |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0043752 | molecular_function | adenosylcobinamide kinase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0008820 | molecular_function | cobinamide phosphate guanylyltransferase activity |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0043752 | molecular_function | adenosylcobinamide kinase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0008820 | molecular_function | cobinamide phosphate guanylyltransferase activity |
| C | 0009236 | biological_process | cobalamin biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0043752 | molecular_function | adenosylcobinamide kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 600 |
| Chain | Residue |
| A | GLY7 |
| A | ARG9 |
| A | SER10 |
| A | GLY11 |
| A | LYS12 |
| A | SER13 |
| A | HOH851 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 601 |
| Chain | Residue |
| B | SER10 |
| B | GLY11 |
| B | LYS12 |
| B | SER13 |
| B | HOH725 |
| B | HOH749 |
| B | GLY7 |
| B | ARG9 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 607 |
| Chain | Residue |
| C | SER13 |
| C | GLU80 |
| C | POP608 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 5GP A 604 |
| Chain | Residue |
| A | TYR28 |
| A | ALA30 |
| A | THR31 |
| A | SER32 |
| A | ILE34 |
| A | ILE43 |
| A | HIS46 |
| A | LYS47 |
| A | ARG50 |
| A | GLU58 |
| A | GLU80 |
| A | CYS81 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 5GP B 605 |
| Chain | Residue |
| B | SER13 |
| B | TYR28 |
| B | ALA30 |
| B | THR31 |
| B | SER32 |
| B | ILE43 |
| B | HIS46 |
| B | LYS47 |
| B | ARG50 |
| B | GLU58 |
| B | GLU80 |
| B | CYS81 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE POP C 608 |
| Chain | Residue |
| C | GLY7 |
| C | ALA8 |
| C | ARG9 |
| C | SER10 |
| C | GLY11 |
| C | LYS12 |
| C | SER13 |
| C | MG607 |
| C | HOH739 |
| C | HOH898 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 5GP C 606 |
| Chain | Residue |
| C | TYR28 |
| C | ALA30 |
| C | THR31 |
| C | SER32 |
| C | ILE34 |
| C | LYS47 |
| C | ARG50 |
| C | GLU80 |
| C | CYS81 |
| C | THR84 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"GMP-histidine intermediate","evidences":[{"source":"PubMed","id":"10529169","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 41 |
| Details | Binding site: {} |
| Chain | Residue | Details |
