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

5CNN

Crystal structure of the EGFR kinase domain mutant I682Q

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 Residues26
Detailsbinding site for residue ANP A 1101
ChainResidue
AGLY695
AGLN767
AMET769
ACYS773
AASP813
AARG817
AASN818
ALEU820
AASP831
AMG1102
AHOH1201
ASER696
AHOH1222
AHOH1253
AHOH1256
AHOH1272
AHOH1274
AHOH1284
AHOH1298
AGLY697
AALA698
AGLY700
AVAL702
AALA719
ALYS721
ATHR766

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 1102
ChainResidue
AASN818
AASP831
AANP1101
AHOH1201
AHOH1272

site_idAC3
Number of Residues26
Detailsbinding site for residue ANP B 1101
ChainResidue
BGLY695
BSER696
BGLY697
BALA698
BPHE699
BGLY700
BVAL702
BALA719
BLYS721
BGLN767
BMET769
BCYS773
BASP813
BARG817
BASN818
BLEU820
BASP831
BMG1102
BHOH1206
BHOH1241
BHOH1259
BHOH1262
BHOH1263
BHOH1268
BHOH1273
BHOH1286

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 1102
ChainResidue
BASN818
BASP831
BANP1101
BHOH1259

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK
ChainResidueDetails
ALEU694-LYS721

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV
ChainResidueDetails
ALEU809-VAL821

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
AASP813
BASP813

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41
ChainResidueDetails
ALEU694
BLEU694

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41
ChainResidueDetails
ALYS721
BLYS721

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41
ChainResidueDetails
ATHR766
BTHR766

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3, ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX, ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN, ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41
ChainResidueDetails
AASP831
BASP831

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for interaction with PIK3C2B
ChainResidueDetails
ATYR992
BTYR992

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
ChainResidueDetails
ALYS721
BLYS721

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:23774213
ChainResidueDetails
ATYR845
BTYR845

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER967
BSER967

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER971
ASER1015
ASER1018
BSER971
BSER1015
BSER1018

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0007744|PubMed:18669648
ChainResidueDetails
ATYR974
BTYR974

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:23774213
ChainResidueDetails
ATYR992
BTYR992

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16083266, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1002
BSER1002

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR1017
BTHR1017

site_idSWS_FT_FI15
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800
ChainResidueDetails
ALYS692
ALYS713
ALYS730
ALYS843
BLYS692
BLYS713
BLYS730
BLYS843

site_idSWS_FT_FI16
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144
ChainResidueDetails
ALYS905
ALYS946
BLYS905
BLYS946

site_idSWS_FT_FI17
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800
ChainResidueDetails
ALYS733
ALYS936
BLYS733
BLYS936

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon