2FV7
Crystal structure of human ribokinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004747 | molecular_function | ribokinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006014 | biological_process | D-ribose metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019303 | biological_process | D-ribose catabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046835 | biological_process | carbohydrate phosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004747 | molecular_function | ribokinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006014 | biological_process | D-ribose metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019303 | biological_process | D-ribose catabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046835 | biological_process | carbohydrate phosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 403 |
| Chain | Residue |
| A | ASP263 |
| A | SER301 |
| A | ALA304 |
| A | SER310 |
| A | HOH878 |
| A | HOH879 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 404 |
| Chain | Residue |
| A | HOH825 |
| A | ADP401 |
| A | HOH817 |
| A | HOH819 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 405 |
| Chain | Residue |
| B | ASP263 |
| B | SER301 |
| B | ALA304 |
| B | SER310 |
| B | HOH845 |
| B | HOH853 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 406 |
| Chain | Residue |
| B | ADP402 |
| B | HOH842 |
| B | HOH859 |
| B | HOH864 |
| B | HOH871 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 401 |
| Chain | Residue |
| A | ASN199 |
| A | THR235 |
| A | LEU236 |
| A | GLY237 |
| A | GLY240 |
| A | THR256 |
| A | GLU257 |
| A | VAL259 |
| A | ALA267 |
| A | GLY268 |
| A | ASN295 |
| A | ALA298 |
| A | VAL302 |
| A | MG404 |
| A | HOH805 |
| A | HOH856 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 402 |
| Chain | Residue |
| B | ASN199 |
| B | THR235 |
| B | LEU236 |
| B | GLY237 |
| B | ALA238 |
| B | GLY240 |
| B | THR256 |
| B | GLU257 |
| B | VAL259 |
| B | GLY268 |
| B | ASN295 |
| B | ALA298 |
| B | MG406 |
| B | HOH871 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UNX A 501 |
| Chain | Residue |
| A | VAL21 |
| A | GLY22 |
| A | CYS151 |
| A | GLN152 |
| A | ILE155 |
| A | SER160 |
| A | HOH801 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX B 502 |
| Chain | Residue |
| B | VAL21 |
| B | GLN152 |
| B | ILE155 |
| B | SER160 |
| B | HOH807 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 503 |
| Chain | Residue |
| B | GLY53 |
| B | ASN57 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 504 |
| Chain | Residue |
| B | LYS173 |
| site_id | BC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 505 |
| Chain | Residue |
| B | ASP78 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 506 |
| Chain | Residue |
| A | LYS173 |
| A | ASP194 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 507 |
| Chain | Residue |
| A | GLY171 |
| B | LYS46 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 510 |
| Chain | Residue |
| A | LYS54 |
| A | ASP269 |
| A | HOH856 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 511 |
| Chain | Residue |
| B | PHE51 |
Functional Information from PROSITE/UniProt
| site_id | PS00584 |
| Number of Residues | 14 |
| Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDsfvGALA |
| Chain | Residue | Details |
| A | ASP263-ALA276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A9J6","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A9J6","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human ribokinase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human ribokinase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| A | GLY266 | |
| A | GLY268 | |
| A | ASP269 | |
| A | ALA267 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rk2 |
| Chain | Residue | Details |
| B | GLY266 | |
| B | GLY268 | |
| B | ASP269 | |
| B | ALA267 |
