2J90
Crystal structure of human ZIP kinase in complex with a tetracyclic pyridone inhibitor (Pyridone 6)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | LYS42 |
| A | ASP161 |
| A | IZA300 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 301 |
| Chain | Residue |
| B | LYS42 |
| B | ASP161 |
| B | IZA300 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| A | LYS133 |
| B | HOH2132 |
| B | HOH2133 |
| A | GLU70 |
| A | ARG72 |
| A | TYR129 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IZA A 300 |
| Chain | Residue |
| A | LEU19 |
| A | VAL27 |
| A | ALA40 |
| A | LYS42 |
| A | GLU94 |
| A | LEU95 |
| A | VAL96 |
| A | ASP161 |
| A | CL301 |
| A | HOH2087 |
| A | HOH2193 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 400 |
| Chain | Residue |
| A | LYS42 |
| A | GLU64 |
| A | HOH2120 |
| A | HOH2121 |
| A | HOH2194 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE IZA B 300 |
| Chain | Residue |
| B | LEU19 |
| B | VAL27 |
| B | ALA40 |
| B | GLU94 |
| B | LEU95 |
| B | VAL96 |
| B | ASP161 |
| B | CL301 |
| B | HOH2038 |
| B | HOH2130 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 400 |
| Chain | Residue |
| B | LYS261 |
| B | ARG263 |
| B | GLN268 |
| B | HOH2131 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 401 |
| Chain | Residue |
| B | ALA25 |
| B | LYS42 |
| B | GLU64 |
| B | HOH2009 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVRkCrqkgtgkeyaak......FIKK |
| Chain | Residue | Details |
| A | LEU19-LYS46 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML |
| Chain | Residue | Details |
| A | ILE135-LEU147 |
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"},{"source":"PROSITE-ProRule","id":"PRU10027","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":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J90","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17158456","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis and ROCK1","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17158456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 43 |
| Details | Region: {"description":"Activation segment","evidences":[{"source":"UniProtKB","id":"O96017","evidenceCode":"ECO:0000250"}]} |
| 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 | GLU143 | |
| A | ASP139 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | GLU143 | |
| B | ASP139 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP139 | |
| A | LYS141 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP139 | |
| B | LYS141 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR180 | |
| A | ASP139 | |
| A | LYS141 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR180 | |
| B | ASP139 | |
| B | LYS141 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP139 | |
| A | LYS141 | |
| A | ASN144 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP139 | |
| B | LYS141 | |
| B | ASN144 |
