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Code : 1F3M   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1
Release Data : 2000-06-29
Compound :
mol_id molecule chains
1 SERINE/THREONINE-PROTEIN KINASE PAK-ALPHA A,B
ec: 2.7.1.-
fragment: PAK1 AUTOREGULATORY DOMAIN (70-149)
mol_id molecule chains
2 SERINE/THREONINE-PROTEIN KINASE PAK-ALPHA C,D
ec: 2.7.1.-
fragment: KINASE DOMAIN (249-545)
mutation: K299R
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PGEX2N
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_vector_type: PLASMID
expression_system_plasmid: PGEX2N
Authors : Lei, M., Lu, W., Meng, W., Parrini, M.-C., Eck, M.J., Mayer, B.J., Harrison, S.C.
Keywords : Kinase domain, autoinhibitory fragment, homodimer, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch.

Lei, M.,Lu, W.,Meng, W.  et al.
(2000)  Cell(Cambridge,Mass.)  102 : 387 - 397

PubMed: 10975528
DOI: 10.1016/S0092-8674(00)00043-X

Chain : C, D
UniProt : Q13153 (PAK1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.1 PubMed:10551809, PubMed:20417602, PubMed:22153498, PubMed:9032240
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ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 PubMed:10551809, PubMed:22153498, PubMed:9032240
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