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
Chain | Residue | Details |
B | GLN427 | |
C | GLN427 | |
Chain | Residue | Details |
B | ILE273 | |
C | ILE273 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
B | LYS296 | |
C | LYS296 | |
Chain | Residue | Details |
B | ARG445 | |
C | ARG445 | |
Chain | Residue | Details |
B | THR258 | |
C | THR258 | |
Chain | Residue | Details |
B | TYR293 | |
C | TYR293 | |
Chain | Residue | Details |
B | GLN459 | |
C | GLN459 | |
Chain | Residue | Details |
B | ASP464 | |
C | ASP464 | |
Chain | Residue | Details |
B | VAL469 | |
C | VAL469 | |
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 | |