6WJZ
Crystal structure of human ribokinase in complex with AMPCP
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 | 25 |
| Details | binding site for residue A12 A 401 |
| Chain | Residue |
| A | ASN199 |
| A | ASN295 |
| A | ALA298 |
| A | ALA299 |
| A | MG408 |
| A | HOH501 |
| A | HOH512 |
| A | HOH514 |
| A | HOH529 |
| A | HOH538 |
| A | HOH543 |
| A | THR235 |
| A | HOH547 |
| A | HOH598 |
| A | HOH601 |
| A | HOH622 |
| A | HOH651 |
| A | HOH655 |
| A | LEU236 |
| A | GLY237 |
| A | GLY240 |
| A | THR256 |
| A | GLU257 |
| A | VAL259 |
| A | ALA267 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ASP27 |
| A | GLY52 |
| A | GLY53 |
| A | LYS54 |
| A | ASN57 |
| A | ALA109 |
| A | GLU154 |
| A | HOH533 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | GLU96 |
| A | ALA214 |
| A | ALA215 |
| A | GLY218 |
| A | PRO251 |
| A | HIS253 |
| A | HOH582 |
| A | HOH644 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | LYS74 |
| A | THR101 |
| A | LEU209 |
| A | THR210 |
| A | HOH507 |
| A | HOH518 |
| A | HOH553 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | LYS173 |
| A | LEU285 |
| A | LEU287 |
| A | MET290 |
| A | HOH570 |
| A | HOH580 |
| A | HOH642 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | LEU130 |
| A | ASN132 |
| A | HOH507 |
| A | HOH575 |
| A | HOH686 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 407 |
| Chain | Residue |
| A | ASP263 |
| A | THR265 |
| A | SER301 |
| A | ALA304 |
| A | SER310 |
| A | HOH571 |
| A | HOH631 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 408 |
| Chain | Residue |
| A | A12401 |
| A | HOH514 |
| A | HOH598 |
| A | HOH601 |
| A | HOH651 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for residue A12 B 401 |
| Chain | Residue |
| B | ASN199 |
| B | THR235 |
| B | LEU236 |
| B | GLY237 |
| B | GLY240 |
| B | THR256 |
| B | GLU257 |
| B | ALA267 |
| B | GLY268 |
| B | ASN295 |
| B | ALA298 |
| B | MG404 |
| B | HOH503 |
| B | HOH521 |
| B | HOH531 |
| B | HOH535 |
| B | HOH588 |
| B | HOH597 |
| B | HOH607 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | ASP27 |
| B | GLY52 |
| B | GLY53 |
| B | ASN57 |
| B | GLU154 |
| B | HOH642 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 403 |
| Chain | Residue |
| B | SER301 |
| B | ALA304 |
| B | SER310 |
| B | HOH519 |
| B | HOH583 |
| B | ASP263 |
| B | THR265 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | A12401 |
| B | HOH521 |
| B | HOH531 |
| B | HOH597 |
| B | HOH623 |
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 |
