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2GS7

Crystal Structure of the inactive EGFR kinase domain in complex with AMP-PNP

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 Residues4
DetailsBINDING SITE FOR RESIDUE MG B 201
ChainResidue
BHOH38
BANP302
BASN818
BASP831

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
AHOH100
AANP301
AASN818
AASP831

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 401
ChainResidue
BGLN825
ALYS715

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 402
ChainResidue
AGLN825

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 403
ChainResidue
ALYS855

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD B 405
ChainResidue
AHOH33
APRO770
BLYS704
BPRO770

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 406
ChainResidue
AVAL810
AARG812

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 407
ChainResidue
BARG812

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 409
ChainResidue
AASN747

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 410
ChainResidue
ATYR891

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 411
ChainResidue
BTYR891

site_idBC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ANP A 301
ChainResidue
AHOH100
AMG202
ALEU694
AGLY695
AGLY697
AVAL702
AALA719
ALYS721
ATHR766
AGLN767
AMET769
AARG817
ALEU820
AASP831

site_idBC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ANP B 302
ChainResidue
BHOH38
BHOH61
BHOH116
BMG201
BLEU694
BGLY695
BGLY697
BALA698
BVAL702
BALA719
BLYS721
BTHR766
BGLN767
BMET769
BARG817
BASN818
BLEU820
BASP831

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER971
BSER971

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 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_FI14
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_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800
ChainResidueDetails
ALYS733
ALYS936
BLYS733
BLYS936

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AARG817
AASP813

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BARG817
BASP813

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP813
AALA815

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP813
BALA815

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP813
AASN818
AALA815

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP813
BASN818
BALA815

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PDB entries from 2024-07-10

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