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3ET7

Crystal structure of PYK2 complexed with PF-2318841

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 349 A 999
ChainResidue
ALEU431
AVAL487
AMET502
AGLU503
ALEU504
ATYR505
AGLU509
AARG553
ALEU556

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A1001
ChainResidue
APRO484
AHIS485

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGFFGEVYeGvytnhkgekin.......VAVK
ChainResidueDetails
ALEU431-LYS457

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDIAVRNILV
ChainResidueDetails
ACYS545-VAL557

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19244237","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FZP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG553
AASP549

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA551
AASP549

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN554
AALA551
AASP549

238895

PDB entries from 2025-07-16

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