Brand  (β version)

PDB ID: 1OKW

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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
FCL 3-chloro-L-phenylalanine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
ACE Acetyl group
NH2 Amino group

Structure summary

Code : 1OKW   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE INHIBITOR
Title : Cyclin A binding groove inhibitor Ac-Arg-Arg-Leu-Asn-(M-Cl-Phe)-NH2
Release Data : 2003-12-11
Compound :
mol_id molecule chains synonym
1 CELL DIVISION PROTEIN KINASE 2 A,C CYCLIN-DEPENDENT KINASE 2, P33 PROTEIN KINASE
ec: 2.7.1.37
mol_id molecule chains synonym
2 CYCLIN A2 B,D CYCLIN A
fragment: RESIDUES 173-432
other_details: CYCLIN GROOVE-BOUND PEPTIDE ACE-ARG-ARG-LEU-ASN-FCL-NH2
mol_id molecule chains
3 ACE-ARG-ARG-LEU-ASN-FCL-NH2 E,F
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN SPODOPTERA FRUGIPERDA  (taxid:7108)
expression_system_common: FALL ARMYWORM
expression_system_vector_type: BACULOVIRUS
mol_id organism_scientific organism_common expression_system
2 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI  (taxid:562)
mol_id organism_scientific
3 SYNTHETIC CONSTRUCT  (taxid:32630)
synthetic: yes
Authors : Kontopidis, G., Andrews, M., McInnes, C., Cowan, A., Powers, H., Innes, L., Plater, A., Griffiths, G., Paterson, D., Zheleva, D., Lane, D., Green, S., Walkinshaw, M., Fischer, P.
Keywords : CELL CYCLE, COMPLEX(KINASE-CYCLIN), CYCLIN A, LIGAND EXCHANGE, PEPTIDOMIMETICS, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Insights Into Cyclin Groove Recognition. Complex Crystal Structures and Inhibitor Design Through Ligand Exchange

Kontopidis, G.,Andrews, M.,Mcinnes, C.  et al.
(2003)  Structure  11 : 1537

PubMed: 14656438
DOI: 10.1016/J.STR.2003.11.006

Reaction

Chain : A, C
UniProt : P24941 (CDK2_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+) 2.7.11.22 PubMed:1396589, PubMed:24670654, PubMed:28216226, PubMed:28666995, PubMed:9030781
-
L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H(+) 2.7.11.22 PubMed:1396589, PubMed:24670654, PubMed:28666995, PubMed:9030781
-
Cofactor: Evidence: Note:
Mg(2+) ECO:0000269 | PubMed:21565702
Binds 2 Mg(2+) ions.
Chain : B, D
UniProt : P20248 (CCNA2_HUMAN)
Reaction : -