5YG8
Crystal structure of ribose-1,5-bisphosphate isomerase from Pyrococcus horikoshii OT3 in complex with ribulose-1,5-bisphosphate, AMP and GMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019323 | biological_process | pentose catabolic process |
| A | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| A | 0044237 | biological_process | cellular metabolic process |
| A | 0044249 | biological_process | cellular biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019323 | biological_process | pentose catabolic process |
| B | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| B | 0044237 | biological_process | cellular metabolic process |
| B | 0044249 | biological_process | cellular biosynthetic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019323 | biological_process | pentose catabolic process |
| C | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| C | 0044237 | biological_process | cellular metabolic process |
| C | 0044249 | biological_process | cellular biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue RUB A 401 |
| Chain | Residue |
| A | MET19 |
| A | ALA139 |
| A | GLN166 |
| A | ALA203 |
| A | ASP204 |
| A | ASN214 |
| A | LYS215 |
| A | LYS240 |
| A | HOH516 |
| A | HOH519 |
| A | HOH527 |
| A | ARG22 |
| A | HOH535 |
| A | GLY23 |
| A | ALA24 |
| A | GLY25 |
| A | ARG65 |
| A | CYS135 |
| A | SER137 |
| A | LYS138 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue MPD A 402 |
| Chain | Residue |
| B | GLU227 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue AMP A 403 |
| Chain | Residue |
| A | ARG124 |
| A | ARG190 |
| A | LYS194 |
| A | ARG229 |
| A | TRP231 |
| A | ASP290 |
| A | HOH501 |
| B | THR207 |
| B | ASN209 |
| B | ALA211 |
| B | LEU250 |
| B | VAL251 |
| B | VAL283 |
| B | HOH504 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue K A 404 |
| Chain | Residue |
| A | MET193 |
| A | LYS194 |
| A | THR196 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue RUB B 401 |
| Chain | Residue |
| B | MET19 |
| B | ARG22 |
| B | GLY23 |
| B | ALA24 |
| B | GLY25 |
| B | ARG65 |
| B | CYS135 |
| B | SER137 |
| B | LYS138 |
| B | ALA139 |
| B | GLN166 |
| B | ASP204 |
| B | ASN214 |
| B | LYS215 |
| B | LYS240 |
| B | HOH511 |
| B | HOH512 |
| B | HOH513 |
| B | HOH518 |
| B | HOH520 |
| B | HOH521 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue AMP B 402 |
| Chain | Residue |
| B | ARG124 |
| B | ARG229 |
| B | TRP231 |
| B | ASP290 |
| B | HOH509 |
| C | ARG190 |
| C | LYS194 |
| C | THR207 |
| C | ASN209 |
| C | ALA211 |
| C | LEU250 |
| C | VAL251 |
| C | VAL283 |
| C | PRO285 |
| C | PRO286 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue K B 403 |
| Chain | Residue |
| B | MET193 |
| B | LYS194 |
| B | THR196 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue 5GP B 404 |
| Chain | Residue |
| B | GLU264 |
| B | ARG268 |
| B | PRO271 |
| B | ILE274 |
| B | GLU275 |
| B | VAL276 |
| B | HOH501 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | binding site for residue RUB C 401 |
| Chain | Residue |
| C | LYS240 |
| C | HOH504 |
| C | HOH515 |
| C | MET19 |
| C | ARG22 |
| C | GLY23 |
| C | ALA24 |
| C | GLY25 |
| C | ARG65 |
| C | CYS135 |
| C | SER137 |
| C | LYS138 |
| C | ALA139 |
| C | GLN166 |
| C | ALA203 |
| C | ASP204 |
| C | ASN214 |
| C | LYS215 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue AMP C 402 |
| Chain | Residue |
| A | ASN209 |
| A | ALA211 |
| A | LEU250 |
| A | VAL251 |
| A | VAL283 |
| A | HOH522 |
| B | ARG190 |
| B | LYS194 |
| C | ARG124 |
| C | ARG229 |
| C | TRP231 |
| C | ASP290 |
| C | HOH502 |
| C | HOH527 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue K C 403 |
| Chain | Residue |
| C | MET193 |
| C | LYS194 |
| C | THR196 |
| C | VAL230 |
| C | HOH541 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue 5GP C 404 |
| Chain | Residue |
| C | GLU264 |
| C | LEU267 |
| C | TRP270 |
| C | PRO271 |
| C | ILE274 |
| C | GLU275 |
| C | VAL276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230 |
| Chain | Residue | Details |
| A | CYS135 | |
| B | CYS135 | |
| C | CYS135 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02230 |
| Chain | Residue | Details |
| A | ASP204 | |
| B | ASP204 | |
| C | ASP204 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230 |
| Chain | Residue | Details |
| A | ARG22 | |
| B | LYS240 | |
| C | ARG22 | |
| C | ARG65 | |
| C | SER137 | |
| C | ASN214 | |
| C | LYS240 | |
| A | ARG65 | |
| A | SER137 | |
| A | ASN214 | |
| A | LYS240 | |
| B | ARG22 | |
| B | ARG65 | |
| B | SER137 | |
| B | ASN214 |
