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2HY8

PAK1 complex with ST2001

Functional Information from GO Data
ChainGOidnamespacecontents
10004672molecular_functionprotein kinase activity
10005524molecular_functionATP binding
10006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 1ST 1 201
ChainResidue
1HOH187
1GLY350
1ASP393
1ASN394
1LEU396
1THR406
1ILE276
1GLY277
1ALA297
1ARG299
1VAL328
1GLU345
1TYR346
1LEU347

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKsdNILL
ChainResidueDetails
1VAL385-LEU397

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:22153498
ChainResidueDetails
1ASP389

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22153498
ChainResidueDetails
1ILE276
1ARG299
1GLU345

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
ChainResidueDetails
1TYR285

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945
ChainResidueDetails
1GLU423

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
1ASP393
1ASP389

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
1LYS391
1ASP389

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
1LYS391
1ASP389
1THR427

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
1LYS391
1ASP389
1ASN394

224572

PDB entries from 2024-09-04

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