3HM8
Crystal structure of the C-terminal Hexokinase domain of human HK3
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001678 | biological_process | intracellular glucose homeostasis |
A | 0004396 | molecular_function | hexokinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005536 | molecular_function | D-glucose binding |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
B | 0001678 | biological_process | intracellular glucose homeostasis |
B | 0004396 | molecular_function | hexokinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005536 | molecular_function | D-glucose binding |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006096 | biological_process | glycolytic process |
B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
C | 0001678 | biological_process | intracellular glucose homeostasis |
C | 0004396 | molecular_function | hexokinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005536 | molecular_function | D-glucose binding |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0006096 | biological_process | glycolytic process |
C | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
D | 0001678 | biological_process | intracellular glucose homeostasis |
D | 0004396 | molecular_function | hexokinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005536 | molecular_function | D-glucose binding |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0006096 | biological_process | glycolytic process |
D | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
Functional Information from PROSITE/UniProt
site_id | PS00378 |
Number of Residues | 26 |
Details | HEXOKINASE_1 Hexokinase domain signature. LGFTFSFPcrqlgLDqgiLlnWTKgF |
Chain | Residue | Details |
A | LEU604-PHE629 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 520 |
Details | Region: {"description":"Hexokinase small subdomain 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01084","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 478 |
Details | Region: {"description":"Hexokinase large subdomain 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01084","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 96 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P19367","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of the C-terminal Hexokinase domain of human HK3.","authors":["Nedyalkova L.","Tong Y.","Rabeh W.","Tempel W.","Landry R.","Arrowsmith C.H.","Edwards A.M.","Bountra C.","Weigelt J.","Bochkarev A.","Park H."]}},{"source":"PDB","id":"3HM8","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |