2VZD
Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex with paxillin LD1 motif
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO D 1015 |
| Chain | Residue |
| B | ASP348 |
| B | ASP353 |
| D | HOH2001 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE A 1373 |
| Chain | Residue |
| A | HIS311 |
| A | PHE313 |
| A | PHE314 |
| A | LEU315 |
| A | LEU325 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG4 A 1374 |
| Chain | Residue |
| A | LEU261 |
| A | PHE320 |
| A | GLU321 |
| A | GLU347 |
| A | ASN351 |
| A | ASP353 |
| A | LEU354 |
| A | LYS355 |
| A | PGE1375 |
| A | GOL1377 |
| A | PHE254 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE A 1375 |
| Chain | Residue |
| A | ARG345 |
| A | ASP348 |
| A | PG41374 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1376 |
| Chain | Residue |
| A | TYR306 |
| A | PHE307 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1377 |
| Chain | Residue |
| A | ARG345 |
| A | GLU347 |
| A | CYS352 |
| A | ASP353 |
| A | LEU354 |
| A | PG41374 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PG4 B 1373 |
| Chain | Residue |
| B | LEU310 |
| B | HIS311 |
| B | PHE313 |
| B | PHE314 |
| B | LEU315 |
| B | PHE320 |
| B | GLU321 |
| B | EDO1378 |
| B | HOH2038 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 1374 |
| Chain | Residue |
| B | LEU279 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1375 |
| Chain | Residue |
| B | SER328 |
| B | SER328 |
| B | PHE329 |
| B | GLU332 |
| B | ARG345 |
| B | GLU347 |
| B | EDO1378 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1378 |
| Chain | Residue |
| A | GLN289 |
| A | ASP292 |
| A | TYR295 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1379 |
| Chain | Residue |
| A | LEU298 |
| A | TYR306 |
| B | VAL308 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1376 |
| Chain | Residue |
| B | ASP292 |
| B | TYR295 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1377 |
| Chain | Residue |
| B | THR288 |
| B | LYS323 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1378 |
| Chain | Residue |
| B | HIS311 |
| B | SER312 |
| B | GLU347 |
| B | PG41373 |
| B | EDO1375 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 214 |
| Details | Domain: {"description":"Calponin-homology (CH) 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"37316325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"37316325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
