5BYC
Crystal structure of human ribokinase in C2 spacegroup
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 | 0006753 | biological_process | nucleoside phosphate metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| 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 | 0006753 | biological_process | nucleoside phosphate metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| 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 401 |
| Chain | Residue |
| A | ASP263 |
| A | SER301 |
| A | ALA304 |
| A | SER310 |
| A | HOH563 |
| A | HOH620 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 401 |
| Chain | Residue |
| B | SER310 |
| B | HOH608 |
| B | HOH612 |
| B | ASP263 |
| B | SER301 |
| B | ALA304 |
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 | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-Rule:MF_03215 |
| Chain | Residue | Details |
| A | ASP269 | |
| B | ASP269 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A9J6, ECO:0000255|HAMAP-Rule:MF_03215 |
| Chain | Residue | Details |
| A | MET25 | |
| B | THR265 | |
| B | ASP269 | |
| B | GLY306 | |
| A | GLY53 | |
| A | GLU154 | |
| A | THR265 | |
| A | ASP269 | |
| A | GLY306 | |
| B | MET25 | |
| B | GLY53 | |
| B | GLU154 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | ASN199 | |
| B | ASN295 | |
| A | THR235 | |
| A | THR256 | |
| A | GLY268 | |
| A | ASN295 | |
| B | ASN199 | |
| B | THR235 | |
| B | THR256 | |
| B | GLY268 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000305|Ref.7 |
| Chain | Residue | Details |
| A | ASP263 | |
| A | SER301 | |
| A | ALA304 | |
| A | SER310 | |
| B | ASP263 | |
| B | SER301 | |
| B | ALA304 | |
| B | SER310 |
