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6GCW

Focal Adhesion Kinase catalytic domain in complex with irreversible inhibitor

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
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue EUQ A 701
ChainResidue
AILE428
ACYS502
AGLY505
AGLU506
ALEU553
BVAL513
BHOH870
AGLY429
AGLU430
AVAL436
AALA452
ALYS454
AMET499
AGLU500
ALEU501

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 702
ChainResidue
ASER601
AARG668
AHOH856
AHOH876

site_idAC3
Number of Residues14
Detailsbinding site for residue EUQ B 701
ChainResidue
AASP630
BILE428
BALA452
BMET499
BGLU500
BLEU501
BCYS502
BGLY505
BLEU553
BGLY563
BASP564
BLEU567
BSER568
BHOH839

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGQFGDVHqGiymspenpama.......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. HrdiaarnvlVSatdCVklgDfgLsrYMeDS
ChainResidueDetails
AHIS544-SER574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP546
BASP546

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AILE428
ALYS454
AGLU500
BILE428
BLYS454
BGLU500

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:12370821, ECO:0000269|PubMed:17574028
ChainResidueDetails
ATYR576
BTYR576

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000250
ChainResidueDetails
ATYR577
BTYR577

222415

PDB entries from 2024-07-10

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