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

4D5H

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 Residues14
DetailsBINDING SITE FOR RESIDUE 9RM A 1687
ChainResidue
AILE428
AGLY505
AGLU506
ALEU553
AGLY563
AHOH2037
AGLY429
AGLU430
AVAL436
AALA452
AMET499
AGLU500
ALEU501
ACYS502

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1687
ChainResidue
ALYS621
AGLN624
BASP519
BLEU520
BASN646
BHOH2037

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1688
ChainResidue
BARG508
BGLN512
BLYS621

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1688
ChainResidue
ASER601
AARG668
AHOH2057
AHOH2080
AHOH2118

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1689
ChainResidue
BHIS480
BLYS673
BHOH2040
BHOH2097

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
AGLU500
BILE428
BLYS454
BGLU500
ALYS454
AILE428

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
BTYR577
ATYR577

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon