3A11
Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016853 | molecular_function | isomerase activity |
A | 0019323 | biological_process | pentose catabolic process |
A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
A | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
A | 0044237 | biological_process | cellular metabolic process |
A | 0044249 | biological_process | cellular biosynthetic process |
A | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019323 | biological_process | pentose catabolic process |
B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
B | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
B | 0044237 | biological_process | cellular metabolic process |
B | 0044249 | biological_process | cellular biosynthetic process |
B | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0019323 | biological_process | pentose catabolic process |
C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
C | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
C | 0044237 | biological_process | cellular metabolic process |
C | 0044249 | biological_process | cellular biosynthetic process |
C | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0019323 | biological_process | pentose catabolic process |
D | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
D | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
D | 0044237 | biological_process | cellular metabolic process |
D | 0044249 | biological_process | cellular biosynthetic process |
D | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
E | 0016853 | molecular_function | isomerase activity |
E | 0019323 | biological_process | pentose catabolic process |
E | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
E | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
E | 0044237 | biological_process | cellular metabolic process |
E | 0044249 | biological_process | cellular biosynthetic process |
E | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
F | 0016853 | molecular_function | isomerase activity |
F | 0019323 | biological_process | pentose catabolic process |
F | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
F | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
F | 0044237 | biological_process | cellular metabolic process |
F | 0044249 | biological_process | cellular biosynthetic process |
F | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG A 401 |
Chain | Residue |
A | LYS224 |
A | ARG227 |
A | VAL228 |
A | TYR286 |
A | ASP288 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG E 401 |
Chain | Residue |
A | GLU285 |
A | TYR286 |
E | LYS224 |
E | ARG227 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG B 401 |
Chain | Residue |
B | LYS224 |
B | VAL228 |
B | THR230 |
B | TYR286 |
B | ASP288 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 411 |
Chain | Residue |
B | ASP304 |
B | HOH678 |
D | ASP304 |
F | ASP304 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG C 401 |
Chain | Residue |
C | LYS224 |
C | ARG227 |
C | VAL228 |
C | GLU285 |
C | ASP288 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG D 401 |
Chain | Residue |
D | LYS224 |
D | ARG227 |
D | VAL228 |
D | ASP288 |
D | HOH619 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG E 411 |
Chain | Residue |
A | ASP304 |
E | ASP304 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEG F 401 |
Chain | Residue |
F | LYS224 |
F | VAL228 |
F | GLU285 |
F | TYR286 |
F | ASP288 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 |
Chain | Residue | Details |
A | CYS133 | |
B | CYS133 | |
C | CYS133 | |
D | CYS133 | |
E | CYS133 | |
F | CYS133 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 |
Chain | Residue | Details |
A | ASP202 | |
B | ASP202 | |
C | ASP202 | |
D | ASP202 | |
E | ASP202 | |
F | ASP202 |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230 |
Chain | Residue | Details |
A | ARG20 | |
D | ARG20 | |
D | SER135 | |
D | ASN212 | |
E | ARG20 | |
E | SER135 | |
E | ASN212 | |
F | ARG20 | |
F | SER135 | |
F | ASN212 | |
A | SER135 | |
A | ASN212 | |
B | ARG20 | |
B | SER135 | |
B | ASN212 | |
C | ARG20 | |
C | SER135 | |
C | ASN212 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 |
Chain | Residue | Details |
A | ARG63 | |
E | LYS238 | |
F | ARG63 | |
F | LYS238 | |
A | LYS238 | |
B | ARG63 | |
B | LYS238 | |
C | ARG63 | |
C | LYS238 | |
D | ARG63 | |
D | LYS238 | |
E | ARG63 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | SITE: Plays a key role in hexamerization |
Chain | Residue | Details |
A | ARG227 | |
B | ARG227 | |
C | ARG227 | |
D | ARG227 | |
E | ARG227 | |
F | ARG227 |