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4D4V

Focal Adhesion Kinase catalytic domain

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 Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 1687
ChainResidue
AHIS482
AGLN529
AHOH2026

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS B 1687
ChainResidue
BGLY431
BGLN432
BPHE433
BGLY434

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 1688
ChainResidue
AHOH2018
AILE428
ALEU553

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1689
ChainResidue
ASER601
AARG668
AHOH2062

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1688
ChainResidue
ALYS621
AGLN624
BASP519
BLEU520
BASN646
BHOH2015

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1689
ChainResidue
BHIS480
BLYS673
BHOH2017

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1690
ChainResidue
BARG508
BGLN512

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KB8 B 1691
ChainResidue
BILE428
BVAL436
BALA452
BLYS454
BMET499
BGLU500
BGLU506
BLEU553
BGLY563
BHOH2010
BHOH2032

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

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PDB entries from 2024-07-10

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