3KMW
Crystal structure of the ILK/alpha-parvin core complex (MgATP)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | HOH15 |
| A | HOH54 |
| A | ASP339 |
| A | ATP502 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP A 502 |
| Chain | Residue |
| A | HOH66 |
| A | HOH101 |
| A | ASN200 |
| A | ASN202 |
| A | HIS203 |
| A | SER204 |
| A | LEU207 |
| A | VAL218 |
| A | LYS220 |
| A | HIS270 |
| A | TRP271 |
| A | MET272 |
| A | ASN279 |
| A | ASP339 |
| A | LYS341 |
| A | HOH461 |
| A | HOH473 |
| A | MG501 |
| A | HOH15 |
| A | HOH23 |
| A | HOH24 |
| A | HOH50 |
| A | HOH64 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20005845, ECO:0000269|PubMed:21524996, ECO:0007744|PDB:3KMW, ECO:0007744|PDB:3REP |
| Chain | Residue | Details |
| A | ASN200 | |
| A | ASN202 | |
| A | SER204 | |
| A | LYS220 | |
| A | HIS270 | |
| A | MET272 | |
| A | ASN279 | |
| A | LYS341 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21524996, ECO:0007744|PDB:3REP |
| Chain | Residue | Details |
| A | HIS203 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20005845, ECO:0007744|PDB:3KMW |
| Chain | Residue | Details |
| A | ASP339 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
| Chain | Residue | Details |
| A | SER186 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PAK1 => ECO:0000269|PubMed:17420447 |
| Chain | Residue | Details |
| A | SER246 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O55222 |
| Chain | Residue | Details |
| A | LYS426 |
