2V7O
Crystal structure of human calcium-calmodulin-dependent protein kinase II gamma
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE DRN A 1303 |
Chain | Residue |
A | LEU20 |
A | GLU140 |
A | ASP157 |
A | HOH2109 |
A | GLY21 |
A | VAL28 |
A | ALA41 |
A | VAL74 |
A | PHE90 |
A | ASP91 |
A | LEU92 |
A | VAL93 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1304 |
Chain | Residue |
A | ASN247 |
A | GLN251 |
A | GLN251 |
A | GLN265 |
A | HIS269 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1305 |
Chain | Residue |
A | TYR231 |
A | ASP232 |
A | PHE233 |
A | ALA258 |
A | HOH2110 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCvkktptqe..........YAAK |
Chain | Residue | Details |
A | LEU20-LYS43 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL |
Chain | Residue | Details |
A | ILE132-LEU144 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | Region: {"description":"Autoinhibitory domain","evidences":[{"source":"PubMed","id":"20668654","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
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_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"16690701","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","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 | ASP136 | |
A | GLU140 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP136 | |
A | LYS138 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP136 | |
A | LYS138 | |
A | THR177 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP136 | |
A | LYS138 | |
A | ASN141 |