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4K9Y

FOCAL ADHESION KINASE Catalytic domain in complex with 1-[4-(6-Amino-purin-9-yl)-phenyl]-3-(5-tert-butyl-2-p-tolyl-2H-pyrazol-3-yl)-urea

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 Residues18
DetailsBINDING SITE FOR RESIDUE K9Y A 701
ChainResidue
AILE428
AGLY563
AASP564
APHE565
AARG569
ATYR570
AHOH828
AHOH843
AHOH866
AHOH927
AGLU471
AMET475
AVAL484
AMET499
AGLU500
ACYS502
APHE542
ALEU553

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGQFGDVHqGiymspenpala.......VAIK
ChainResidueDetails
AILE428-LYS454

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDIAARNVLV
ChainResidueDetails
APHE542-VAL554

site_idPS00661
Number of Residues31
DetailsFERM_2 FERM domain signature 2. HrdiaarnvlVSsndCVklgDfgLsrYMeDS
ChainResidueDetails
AHIS544-SER574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP546

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12467573
ChainResidueDetails
AILE428
ALYS454
AGLU500

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR570

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by RET and SRC => ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698
ChainResidueDetails
ATYR576

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by RET and SRC => ECO:0000269|PubMed:12387730, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698
ChainResidueDetails
ATYR577

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER580

223166

PDB entries from 2024-07-31

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