1RK2
E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP, SOLVED IN SPACE GROUP P212121
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004747 | molecular_function | ribokinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006014 | biological_process | D-ribose metabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0019303 | biological_process | D-ribose catabolic process |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046835 | biological_process | carbohydrate phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0004747 | molecular_function | ribokinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006014 | biological_process | D-ribose metabolic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0019303 | biological_process | D-ribose catabolic process |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046835 | biological_process | carbohydrate phosphorylation |
B | 0046872 | molecular_function | metal ion binding |
C | 0004747 | molecular_function | ribokinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006014 | biological_process | D-ribose metabolic process |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0019303 | biological_process | D-ribose catabolic process |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046835 | biological_process | carbohydrate phosphorylation |
C | 0046872 | molecular_function | metal ion binding |
D | 0004747 | molecular_function | ribokinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006014 | biological_process | D-ribose metabolic process |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
D | 0019303 | biological_process | D-ribose catabolic process |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046835 | biological_process | carbohydrate phosphorylation |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00584 |
Number of Residues | 14 |
Details | PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiAAGDtfnGALI |
Chain | Residue | Details |
A | ASP249-ILE262 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 |
Chain | Residue | Details |
A | ASP255 | |
B | ASP255 | |
C | ASP255 | |
D | ASP255 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409 |
Chain | Residue | Details |
A | ASN14 | |
B | GLU143 | |
B | ASN187 | |
B | THR223 | |
B | ASP255 | |
B | HIS279 | |
C | ASN14 | |
C | GLY42 | |
C | GLU143 | |
C | ASN187 | |
C | THR223 | |
A | GLY42 | |
C | ASP255 | |
C | HIS279 | |
D | ASN14 | |
D | GLY42 | |
D | GLU143 | |
D | ASN187 | |
D | THR223 | |
D | ASP255 | |
D | HIS279 | |
A | GLU143 | |
A | ASN187 | |
A | THR223 | |
A | ASP255 | |
A | HIS279 | |
B | ASN14 | |
B | GLY42 |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021 |
Chain | Residue | Details |
A | ASP249 | |
B | ARG288 | |
B | GLY290 | |
B | SER294 | |
C | ASP249 | |
C | ILE251 | |
C | ALA285 | |
C | ARG288 | |
C | GLY290 | |
C | SER294 | |
D | ASP249 | |
A | ILE251 | |
D | ILE251 | |
D | ALA285 | |
D | ARG288 | |
D | GLY290 | |
D | SER294 | |
A | ALA285 | |
A | ARG288 | |
A | GLY290 | |
A | SER294 | |
B | ASP249 | |
B | ILE251 | |
B | ALA285 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021 |
Chain | Residue | Details |
A | GLY254 | |
B | GLY254 | |
C | GLY254 | |
D | GLY254 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 9519409 |
Chain | Residue | Details |
A | GLY254 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 663 |
Chain | Residue | Details |
A | ALA252 | electrostatic stabiliser, polar interaction |
A | ALA253 | electrostatic stabiliser, polar interaction |
A | GLY254 | electrostatic stabiliser, polar interaction |
A | ASP255 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 663 |
Chain | Residue | Details |
B | ALA252 | electrostatic stabiliser, polar interaction |
B | ALA253 | electrostatic stabiliser, polar interaction |
B | GLY254 | electrostatic stabiliser, polar interaction |
B | ASP255 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 663 |
Chain | Residue | Details |
C | ALA252 | electrostatic stabiliser, polar interaction |
C | ALA253 | electrostatic stabiliser, polar interaction |
C | GLY254 | electrostatic stabiliser, polar interaction |
C | ASP255 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 663 |
Chain | Residue | Details |
D | ALA252 | electrostatic stabiliser, polar interaction |
D | ALA253 | electrostatic stabiliser, polar interaction |
D | GLY254 | electrostatic stabiliser, polar interaction |
D | ASP255 | electrostatic stabiliser, proton acceptor, proton donor |