3S95
Crystal structure of the human LIMK1 kinase domain in complex with staurosporine
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE STU A 1 |
| Chain | Residue |
| A | LEU345 |
| A | ILE416 |
| A | GLY419 |
| A | THR420 |
| A | HIS464 |
| A | ASN465 |
| A | LEU467 |
| A | HOH681 |
| A | GLY346 |
| A | VAL366 |
| A | LYS368 |
| A | GLU384 |
| A | LEU397 |
| A | THR413 |
| A | GLU414 |
| A | TYR415 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE STU B 1 |
| Chain | Residue |
| B | LEU345 |
| B | GLY346 |
| B | ALA353 |
| B | VAL366 |
| B | LYS368 |
| B | GLU384 |
| B | THR413 |
| B | GLU414 |
| B | TYR415 |
| B | ILE416 |
| B | GLY419 |
| B | THR420 |
| B | HIS464 |
| B | ASN465 |
| B | LEU467 |
| B | HOH707 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 638 |
| Chain | Residue |
| A | ASN574 |
| B | HOH47 |
| B | HOH202 |
| B | LEU391 |
| B | GLU392 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 2 |
| Chain | Residue |
| A | HOH44 |
| A | HOH254 |
| A | LEU391 |
| A | GLU392 |
| B | ASN574 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 638 |
| Chain | Residue |
| A | MET0 |
| B | LEU567 |
| B | ASP568 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 2 |
| Chain | Residue |
| B | HOH83 |
| B | HIS452 |
| B | SER453 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 3 |
| Chain | Residue |
| A | HOH80 |
| A | HOH263 |
| A | GLY544 |
| A | ARG545 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 4 |
| Chain | Residue |
| A | PRO513 |
| A | TYR514 |
| A | PRO550 |
| A | HOH758 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 5 |
| Chain | Residue |
| A | HOH263 |
| A | ARG569 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 6 |
| Chain | Residue |
| A | HOH37 |
| A | ARG585 |
| A | GLU592 |
| A | LYS593 |
| A | ARG594 |
| A | LYS599 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 7 |
| Chain | Residue |
| A | PRO619 |
| A | GLN620 |
| A | GLN623 |
| B | ILE521 |
| B | ARG555 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 8 |
| Chain | Residue |
| A | HIS602 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 9 |
| Chain | Residue |
| A | SER-1 |
| B | ASP568 |
| B | ARG569 |
| B | CYS571 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 10 |
| Chain | Residue |
| B | HOH124 |
| B | HIS602 |
| B | HOH774 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 11 |
| Chain | Residue |
| A | ASP568 |
| A | ARG569 |
| A | CYS571 |
| B | SER-1 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MRD B 639 |
| Chain | Residue |
| A | HOH36 |
| A | HOH50 |
| A | PRO550 |
| A | ASP551 |
| A | TYR552 |
| B | LYS599 |
| B | HIS602 |
| B | GLN620 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 639 |
| Chain | Residue |
| A | PRO619 |
| A | GLN620 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 640 |
| Chain | Residue |
| B | HOH24 |
| B | HOH131 |
| B | ARG437 |
| B | ARG545 |
| B | PRO572 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS B 641 |
| Chain | Residue |
| B | HIS464 |
| B | HOH690 |
| B | HOH768 |
| B | HOH201 |
| B | ARG422 |
| B | LYS426 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TRS A 640 |
| Chain | Residue |
| A | ARG422 |
| A | LYS426 |
| A | HIS464 |
| A | ASN547 |
| A | HOH740 |
| A | HOH778 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGCFGQAIkVthretgev..........MVMK |
| Chain | Residue | Details |
| A | LEU345-LYS368 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by ROCK1 and PAK1","evidences":[{"source":"PubMed","id":"10559936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10652353","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15660133","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23633677","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
