3GGF
Crystal structure of human Serine/threonine-protein kinase MST4 in complex with an quinazolin
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 301 |
| Chain | Residue |
| A | GLU70 |
| A | HIS142 |
| A | VAL165 |
| A | HOH306 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 302 |
| Chain | Residue |
| A | CYS77 |
| A | HIS136 |
| A | GLU138 |
| A | ASP242 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 303 |
| Chain | Residue |
| A | SER300 |
| A | HOH307 |
| A | GLU267 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 304 |
| Chain | Residue |
| A | ASP109 |
| A | GVD305 |
| A | HOH359 |
| A | HOH360 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GVD A 305 |
| Chain | Residue |
| A | ILE30 |
| A | ALA51 |
| A | LYS53 |
| A | MET99 |
| A | GLU100 |
| A | TYR101 |
| A | LEU102 |
| A | ASP109 |
| A | ALA148 |
| A | ASN149 |
| A | LEU151 |
| A | CD304 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 301 |
| Chain | Residue |
| B | GLU70 |
| B | HIS142 |
| B | VAL165 |
| B | HOH305 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 302 |
| Chain | Residue |
| B | CYS77 |
| B | HIS136 |
| B | GLU138 |
| B | ASP242 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 303 |
| Chain | Residue |
| B | ILE30 |
| B | ASP109 |
| B | GVD304 |
| B | HOH357 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GVD B 304 |
| Chain | Residue |
| B | ILE30 |
| B | VAL38 |
| B | ALA51 |
| B | MET99 |
| B | GLU100 |
| B | TYR101 |
| B | LEU102 |
| B | ASP109 |
| B | ALA148 |
| B | LEU151 |
| B | CD303 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGEVFkGidnrtqqv..........VAIK |
| Chain | Residue | Details |
| A | ILE30-LYS53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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 | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29232556","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"15037601","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA148 | |
| A | ASP144 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ALA148 | |
| B | ASP144 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP144 | |
| A | LYS146 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP144 | |
| B | LYS146 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR182 | |
| A | ASP144 | |
| A | LYS146 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR182 | |
| B | ASP144 | |
| B | LYS146 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN149 | |
| A | ASP144 | |
| A | LYS146 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN149 | |
| B | ASP144 | |
| B | LYS146 |
