1U2E
Crystal Structure of the C-C bond hydrolase MhpC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018771 | molecular_function | 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity |
| A | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| A | 0019622 | biological_process | 3-(3-hydroxy)phenylpropionate catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0052823 | molecular_function | 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018771 | molecular_function | 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity |
| B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| B | 0019622 | biological_process | 3-(3-hydroxy)phenylpropionate catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0052823 | molecular_function | 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0018771 | molecular_function | 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity |
| C | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| C | 0019622 | biological_process | 3-(3-hydroxy)phenylpropionate catabolic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0052823 | molecular_function | 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0018771 | molecular_function | 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity |
| D | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| D | 0019622 | biological_process | 3-(3-hydroxy)phenylpropionate catabolic process |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0052823 | molecular_function | 2-hydroxy-6-oxonona-2,4,7-trienedioate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 1001 |
| Chain | Residue |
| D | GLY3041 |
| D | ALA3044 |
| D | ASN3049 |
| D | ARG3188 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1002 |
| Chain | Residue |
| A | GLY41 |
| A | ALA44 |
| A | ARG188 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1003 |
| Chain | Residue |
| C | ALA2044 |
| C | ARG2188 |
| C | HOH215 |
| C | GLY2041 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1285 |
| Chain | Residue |
| B | GLY1039 |
| B | GLY1041 |
| B | ASN1049 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01654","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15663941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01654","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15663941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Catalytic role in ketonization of the dienol substrate (substrate destabilization)","evidences":[{"source":"HAMAP-Rule","id":"MF_01654","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15663941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17029402","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| A | HIS263 | |
| A | SER110 | |
| A | ASP235 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| B | HIS1263 | |
| B | ASP1235 | |
| B | SER1110 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| C | ASP2235 | |
| C | SER2110 | |
| C | HIS2263 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azw |
| Chain | Residue | Details |
| D | ASP3235 | |
| D | HIS3263 | |
| D | SER3110 |
