4FIG
Catalytic domain of human PAK4
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ANP A 1001 |
Chain | Residue |
A | GLU329 |
A | LEU398 |
A | ASP440 |
A | LEU447 |
A | ASP458 |
A | GLY460 |
A | PHE461 |
A | MG1002 |
A | GLY330 |
A | SER331 |
A | THR332 |
A | VAL335 |
A | LYS350 |
A | GLU366 |
A | GLU396 |
A | PHE397 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG A 1002 |
Chain | Residue |
A | ANP1001 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | ANP602 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ANP B 602 |
Chain | Residue |
B | GLU329 |
B | GLY330 |
B | SER331 |
B | THR332 |
B | VAL335 |
B | LYS350 |
B | GLU366 |
B | MET395 |
B | GLU396 |
B | LEU398 |
B | ASP440 |
B | LEU447 |
B | ASP458 |
B | GLY460 |
B | PHE461 |
B | MG601 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSTGIVCiAtvrssgklv.........AVKK |
Chain | Residue | Details |
A | ILE327-LYS351 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ASP440 | |
B | ASP440 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU |
Chain | Residue | Details |
A | ILE327 | |
A | LYS350 | |
B | ILE327 | |
B | LYS350 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU |
Chain | Residue | Details |
A | GLU396 | |
A | ASP458 | |
B | GLU396 | |
B | ASP458 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | PRO314 | |
B | PRO314 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
A | LYS351 | |
B | LYS351 |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | ASN377 | |
B | SER291 | |
A | CYS421 | |
A | ASP440 | |
A | LEU531 | |
A | SER291 | |
B | ASN377 | |
B | CYS421 | |
B | ASP440 | |
B | LEU531 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | VAL454 | |
B | VAL454 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | GLY460 | |
B | GLY460 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | GLU468 | |
B | GLU468 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | TYR480 | |
B | TYR480 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976 |
Chain | Residue | Details |
A | LYS540 | |
B | LYS540 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|Ref.32, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SEP474 | |
B | SEP474 |