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6TY4

FAK structure with AMP-PNP from single particle analysis of 2D crystals

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0005856cellular_componentcytoskeleton
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005524molecular_functionATP binding
B0005856cellular_componentcytoskeleton
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 701
ChainResidue
AASP564
AANP702

site_idAC2
Number of Residues15
Detailsbinding site for residue ANP A 702
ChainResidue
ALEU501
ACYS502
AGLU506
AARG550
AASN551
ALEU553
AASP564
AMG701
AGLY429
AGLU430
AGLY431
AGLN432
AVAL436
ALYS454
AGLU500

site_idAC3
Number of Residues2
Detailsbinding site for residue MG B 701
ChainResidue
BASP564
BANP702

site_idAC4
Number of Residues15
Detailsbinding site for residue ANP B 702
ChainResidue
BGLY429
BGLU430
BGLY431
BGLN432
BVAL436
BLYS454
BGLU500
BLEU501
BCYS502
BGLU506
BARG550
BASN551
BLEU553
BASP564
BMG701

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 autocatalysis => ECO:0000269|PubMed:12370821
ChainResidueDetails
ATYR397
BTYR397

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250
ChainResidueDetails
ATYR407
BTYR407

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:12370821, ECO:0000269|PubMed:17574028
ChainResidueDetails
ATYR576
BTYR576

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000250
ChainResidueDetails
ATYR577
BTYR577

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PDB entries from 2024-07-17

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