3IKH
Crystal structure of Ribokinase in Complex with ATP and glycerol in the active site from Klebsiella pneumoniae
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 | 0006014 | biological_process | D-ribose metabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0019303 | biological_process | D-ribose catabolic process |
A | 0044281 | biological_process | small molecule metabolic process |
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 | 0006014 | biological_process | D-ribose metabolic process |
B | 0016301 | molecular_function | kinase activity |
B | 0019303 | biological_process | D-ribose catabolic process |
B | 0044281 | biological_process | small molecule metabolic process |
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 | 0006014 | biological_process | D-ribose metabolic process |
C | 0016301 | molecular_function | kinase activity |
C | 0019303 | biological_process | D-ribose catabolic process |
C | 0044281 | biological_process | small molecule metabolic process |
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 | 0006014 | biological_process | D-ribose metabolic process |
D | 0016301 | molecular_function | kinase activity |
D | 0019303 | biological_process | D-ribose catabolic process |
D | 0044281 | biological_process | small molecule metabolic process |
D | 0046835 | biological_process | carbohydrate phosphorylation |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ATP A 900 |
Chain | Residue |
A | ASN182 |
A | HOH328 |
A | HOH331 |
A | HOH346 |
A | HOH360 |
A | HOH390 |
A | THR200 |
A | GLY202 |
A | GLY205 |
A | VAL220 |
A | GLY231 |
A | PHE234 |
A | ALA261 |
A | HOH306 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP B 900 |
Chain | Residue |
B | LYS39 |
B | ASN182 |
B | THR200 |
B | GLN201 |
B | GLY202 |
B | ALA203 |
B | GLY205 |
B | VAL220 |
B | ALA230 |
B | GLY231 |
B | PHE234 |
B | ALA261 |
B | HOH302 |
B | HOH308 |
B | HOH311 |
B | HOH317 |
B | HOH319 |
B | HOH324 |
B | HOH344 |
B | HOH358 |
B | HOH370 |
B | HOH375 |
B | HOH395 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP C 900 |
Chain | Residue |
C | ASN182 |
C | THR200 |
C | GLN201 |
C | GLY202 |
C | ALA203 |
C | GLY205 |
C | VAL220 |
C | GLY229 |
C | ALA230 |
C | GLY231 |
C | PHE234 |
C | ALA261 |
C | HOH300 |
C | HOH303 |
C | HOH304 |
C | HOH330 |
C | HOH336 |
C | HOH360 |
C | HOH377 |
C | HOH387 |
C | HOH388 |
C | HOH391 |
C | HOH393 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 501 |
Chain | Residue |
C | THR10 |
C | ASP12 |
C | GLY38 |
C | ASN42 |
C | SER93 |
C | ASP232 |
C | HOH330 |
C | HOH367 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ATP D 900 |
Chain | Residue |
D | LYS39 |
D | ASN182 |
D | THR200 |
D | GLN201 |
D | GLY202 |
D | ALA203 |
D | GLY205 |
D | VAL220 |
D | ALA230 |
D | GLY231 |
D | PHE234 |
D | ALA261 |
D | HOH300 |
D | HOH316 |
D | HOH328 |
D | HOH334 |
D | HOH353 |
D | HOH356 |
D | HOH358 |
D | HOH361 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 501 |
Chain | Residue |
D | THR10 |
D | ASP12 |
D | GLY38 |
D | ASN42 |
D | SER93 |
D | ASP232 |
D | HOH356 |
Functional Information from PROSITE/UniProt
site_id | PS00583 |
Number of Residues | 25 |
Details | PFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGkGaNQAiiLsRCGietrliaatG |
Chain | Residue | Details |
A | GLY37-GLY61 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
A | GLY231 | |
A | GLY229 | |
A | ASP232 | |
A | ALA230 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
B | GLY231 | |
B | GLY229 | |
B | ASP232 | |
B | ALA230 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
C | GLY231 | |
C | GLY229 | |
C | ASP232 | |
C | ALA230 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rk2 |
Chain | Residue | Details |
D | GLY231 | |
D | GLY229 | |
D | ASP232 | |
D | ALA230 |