Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003743 | molecular_function | translation initiation factor activity |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG B 1641 |
Chain | Residue |
B | ASP432 |
B | ANP1640 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1642 |
Chain | Residue |
B | ASN419 |
B | ASP432 |
B | ANP1640 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 2642 |
Chain | Residue |
C | ASN419 |
C | ASP432 |
C | ANP2640 |
C | MG2641 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 2641 |
Chain | Residue |
C | ASP414 |
C | ASP432 |
C | ANP2640 |
C | MG2642 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 C 901 |
Chain | Residue |
C | LYS304 |
C | ARG307 |
C | ARG413 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ANP B 1640 |
Chain | Residue |
B | GLY279 |
B | VAL281 |
B | VAL294 |
B | LYS296 |
B | MET366 |
B | GLU367 |
B | CYS369 |
B | SER418 |
B | ASN419 |
B | PHE421 |
B | ASP432 |
B | MG1641 |
B | MG1642 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ANP C 2640 |
Chain | Residue |
C | HOH36 |
C | ILE273 |
C | GLY274 |
C | VAL294 |
C | GLU367 |
C | PHE368 |
C | CYS369 |
C | PHE421 |
C | MG2641 |
C | MG2642 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGFGQVFkAkhridgkt..........YVIK |
Chain | Residue | Details |
B | ILE273-LYS296 | |
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"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {} |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16179258","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31246429","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11152499","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16373505","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11337501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16179258","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11337501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20685959","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP414 | |
B | SER418 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASP414 | |
C | SER418 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP414 | |
B | LYS416 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASP414 | |
C | LYS416 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP414 | |
B | LYS416 | |
B | THR451 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN419 | |
B | ASP414 | |
B | LYS416 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASN419 | |
C | ASP414 | |
C | LYS416 | |