1TMH
MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004807 | molecular_function | triose-phosphate isomerase activity |
| A | 0006096 | biological_process | glycolytic process |
| B | 0004807 | molecular_function | triose-phosphate isomerase activity |
| B | 0006096 | biological_process | glycolytic process |
| C | 0004807 | molecular_function | triose-phosphate isomerase activity |
| C | 0006096 | biological_process | glycolytic process |
| D | 0004807 | molecular_function | triose-phosphate isomerase activity |
| D | 0006096 | biological_process | glycolytic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 555 |
| Chain | Residue |
| A | ILE174 |
| A | GLY175 |
| A | GLY213 |
| A | SER214 |
| A | GLY235 |
| A | GLY236 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 556 |
| Chain | Residue |
| B | GLY235 |
| B | GLY236 |
| B | ILE174 |
| B | GLY175 |
| B | SER214 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 557 |
| Chain | Residue |
| C | ILE174 |
| C | GLY175 |
| C | SER214 |
| C | GLY235 |
| C | GLY236 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 558 |
| Chain | Residue |
| D | LYS13 |
| D | ILE174 |
| D | GLY175 |
| D | SER214 |
| D | GLY235 |
| D | GLY236 |
Functional Information from PROSITE/UniProt
| site_id | PS00171 |
| Number of Residues | 11 |
| Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
| Chain | Residue | Details |
| A | ALA167-GLY177 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Electrophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| A | HIS97 | |
| A | LYS13 | |
| A | GLY175 | |
| A | GLU169 | |
| A | ASN11 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| B | HIS97 | |
| B | LYS13 | |
| B | GLY175 | |
| B | GLU169 | |
| B | ASN11 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| C | HIS97 | |
| C | LYS13 | |
| C | GLY175 | |
| C | GLU169 | |
| C | ASN11 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| D | HIS97 | |
| D | LYS13 | |
| D | GLY175 | |
| D | GLU169 | |
| D | ASN11 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 324 |
| Chain | Residue | Details |
| A | ASN11 | electrostatic stabiliser |
| A | LYS13 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS97 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU99 | proton acceptor, proton donor, steric role |
| A | GLU169 | activator, proton acceptor, proton donor |
| A | GLY175 | electrostatic stabiliser |
| A | SER214 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 324 |
| Chain | Residue | Details |
| B | ASN11 | electrostatic stabiliser |
| B | LYS13 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS97 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU99 | proton acceptor, proton donor, steric role |
| B | GLU169 | activator, proton acceptor, proton donor |
| B | GLY175 | electrostatic stabiliser |
| B | SER214 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 324 |
| Chain | Residue | Details |
| C | ASN11 | electrostatic stabiliser |
| C | LYS13 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | HIS97 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLU99 | proton acceptor, proton donor, steric role |
| C | GLU169 | activator, proton acceptor, proton donor |
| C | GLY175 | electrostatic stabiliser |
| C | SER214 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 324 |
| Chain | Residue | Details |
| D | ASN11 | electrostatic stabiliser |
| D | LYS13 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| D | HIS97 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLU99 | proton acceptor, proton donor, steric role |
| D | GLU169 | activator, proton acceptor, proton donor |
| D | GLY175 | electrostatic stabiliser |
| D | SER214 | electrostatic stabiliser, hydrogen bond donor |
