Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YXV

FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH N-Methyl-N-{3-[(2-phenylamino-5-trifluoromethyl-pyrimidin-4-ylamino)-methyl]-pyridin-2-yl}-methanesulfonamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue Q2H A 701
ChainResidue
AILE428
AARG550
AASN551
ALEU553
AGLY563
AASP564
ALEU567
ASER568
AGLU430
AVAL436
AALA452
AVAL484
AMET499
AGLU500
ALEU501
ACYS502

site_idAC2
Number of Residues15
Detailsbinding site for residue Q2H B 701
ChainResidue
BARG426
BGLU430
BALA452
BVAL484
BMET499
BGLU500
BLEU501
BCYS502
BGLY505
BASN551
BLEU553
BGLY563
BASP564
BLEU567
BSER568

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 B 702
ChainResidue
BSER601
BARG668
CSER601
CARG668

site_idAC4
Number of Residues15
Detailsbinding site for residue Q2H C 701
ChainResidue
CARG426
CILE428
CGLU430
CVAL436
CALA452
CMET499
CGLU500
CCYS502
CGLY505
CASN551
CLEU553
CGLY563
CASP564
CLEU567
CSER568

site_idAC5
Number of Residues13
Detailsbinding site for residue Q2H D 701
ChainResidue
DILE428
DVAL436
DMET499
DGLU500
DLEU501
DCYS502
DGLY505
DASN551
DLEU553
DGLY563
DASP564
DLEU567
DSER568

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP546
BASP546
CASP546
DASP546

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12467573
ChainResidueDetails
AILE428
DILE428
DLYS454
DGLU500
ALYS454
AGLU500
BILE428
BLYS454
BGLU500
CILE428
CLYS454
CGLU500

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR570
BTYR570
CTYR570
DTYR570

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by RET and SRC => ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698
ChainResidueDetails
ATYR576
BTYR576
CTYR576
DTYR576

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by RET and SRC => ECO:0000269|PubMed:12387730, ECO:0000269|PubMed:19339212, ECO:0000269|PubMed:21454698
ChainResidueDetails
ATYR577
BTYR577
CTYR577
DTYR577

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER580
BSER580
CSER580
DSER580

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon