1D8W
L-RHAMNOSE ISOMERASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008740 | molecular_function | L-rhamnose isomerase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0019299 | biological_process | rhamnose metabolic process |
A | 0019301 | biological_process | rhamnose catabolic process |
A | 0019324 | biological_process | L-lyxose metabolic process |
A | 0030145 | molecular_function | manganese ion binding |
A | 0032991 | cellular_component | protein-containing complex |
A | 0033296 | molecular_function | rhamnose binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051289 | biological_process | protein homotetramerization |
B | 0005737 | cellular_component | cytoplasm |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008740 | molecular_function | L-rhamnose isomerase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019299 | biological_process | rhamnose metabolic process |
B | 0019301 | biological_process | rhamnose catabolic process |
B | 0019324 | biological_process | L-lyxose metabolic process |
B | 0030145 | molecular_function | manganese ion binding |
B | 0032991 | cellular_component | protein-containing complex |
B | 0033296 | molecular_function | rhamnose binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051289 | biological_process | protein homotetramerization |
C | 0005737 | cellular_component | cytoplasm |
C | 0008270 | molecular_function | zinc ion binding |
C | 0008740 | molecular_function | L-rhamnose isomerase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0019299 | biological_process | rhamnose metabolic process |
C | 0019301 | biological_process | rhamnose catabolic process |
C | 0019324 | biological_process | L-lyxose metabolic process |
C | 0030145 | molecular_function | manganese ion binding |
C | 0032991 | cellular_component | protein-containing complex |
C | 0033296 | molecular_function | rhamnose binding |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051289 | biological_process | protein homotetramerization |
D | 0005737 | cellular_component | cytoplasm |
D | 0008270 | molecular_function | zinc ion binding |
D | 0008740 | molecular_function | L-rhamnose isomerase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0019299 | biological_process | rhamnose metabolic process |
D | 0019301 | biological_process | rhamnose catabolic process |
D | 0019324 | biological_process | L-lyxose metabolic process |
D | 0030145 | molecular_function | manganese ion binding |
D | 0032991 | cellular_component | protein-containing complex |
D | 0033296 | molecular_function | rhamnose binding |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 450 |
Chain | Residue |
A | GLU234 |
A | ASP267 |
A | HIS294 |
A | ASP334 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 450 |
Chain | Residue |
B | GLU234 |
B | ASP267 |
B | HIS294 |
B | ASP334 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 450 |
Chain | Residue |
C | ASP267 |
C | HIS294 |
C | ASP334 |
C | GLU234 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 450 |
Chain | Residue |
D | GLU234 |
D | ASP267 |
D | HIS294 |
D | ASP334 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10891278, ECO:0007744|PDB:1DE6 |
Chain | Residue | Details |
A | HIS103 | |
B | HIS103 | |
C | HIS103 | |
D | HIS103 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10891278, ECO:0007744|PDB:1D8W, ECO:0007744|PDB:1DE5, ECO:0007744|PDB:1DE6 |
Chain | Residue | Details |
A | GLU234 | |
C | ASP267 | |
C | HIS294 | |
C | ASP334 | |
D | GLU234 | |
D | ASP267 | |
D | HIS294 | |
D | ASP334 | |
A | ASP267 | |
A | HIS294 | |
A | ASP334 | |
B | GLU234 | |
B | ASP267 | |
B | HIS294 | |
B | ASP334 | |
C | GLU234 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00541, ECO:0000269|PubMed:10891278, ECO:0007744|PDB:1DE6 |
Chain | Residue | Details |
A | HIS270 | |
D | HIS270 | |
D | ASP302 | |
D | ASP304 | |
A | ASP302 | |
A | ASP304 | |
B | HIS270 | |
B | ASP302 | |
B | ASP304 | |
C | HIS270 | |
C | ASP302 | |
C | ASP304 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1de6 |
Chain | Residue | Details |
A | ASP302 | |
A | LYS236 | |
A | HIS270 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1de6 |
Chain | Residue | Details |
B | ASP302 | |
B | LYS236 | |
B | HIS270 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1de6 |
Chain | Residue | Details |
C | ASP302 | |
C | LYS236 | |
C | HIS270 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1de6 |
Chain | Residue | Details |
D | ASP302 | |
D | LYS236 | |
D | HIS270 |
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 488 |
Chain | Residue | Details |
A | TRP193 | activator |
A | GLU234 | metal ligand |
A | LYS236 | activator |
A | ASP267 | metal ligand |
A | HIS270 | activator, metal ligand |
A | HIS294 | metal ligand |
A | ASP302 | metal ligand |
A | ASP304 | metal ligand, proton acceptor, proton donor |
A | ASP334 | metal ligand, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 488 |
Chain | Residue | Details |
B | TRP193 | activator |
B | GLU234 | metal ligand |
B | LYS236 | activator |
B | ASP267 | metal ligand |
B | HIS270 | activator, metal ligand |
B | HIS294 | metal ligand |
B | ASP302 | metal ligand |
B | ASP304 | metal ligand, proton acceptor, proton donor |
B | ASP334 | metal ligand, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 9 |
Details | M-CSA 488 |
Chain | Residue | Details |
C | TRP193 | activator |
C | GLU234 | metal ligand |
C | LYS236 | activator |
C | ASP267 | metal ligand |
C | HIS270 | activator, metal ligand |
C | HIS294 | metal ligand |
C | ASP302 | metal ligand |
C | ASP304 | metal ligand, proton acceptor, proton donor |
C | ASP334 | metal ligand, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 9 |
Details | M-CSA 488 |
Chain | Residue | Details |
D | TRP193 | activator |
D | GLU234 | metal ligand |
D | LYS236 | activator |
D | ASP267 | metal ligand |
D | HIS270 | activator, metal ligand |
D | HIS294 | metal ligand |
D | ASP302 | metal ligand |
D | ASP304 | metal ligand, proton acceptor, proton donor |
D | ASP334 | metal ligand, proton acceptor, proton donor |