eF-site ID 5czi-AB
PDB Code 5czi
Chain A, B

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Title EGFR L858R MUTANT IN COMPLEX WITH A SHC PEPTIDE SUBSTRATE
Classification TRANSFERASE
Compound Epidermal growth factor receptor
Source Homo sapiens (Human) (5CZI)
Sequence A:  GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEG
EKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVC
RLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLL
NWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITD
FGRAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQS
DVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQ
PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDP
QRYLVIQGDERMHLPDEDMDDVVDADEYLI
B:  DHQYXND
Description


Functional site

1) chain B
residue 105
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:8939605, ECO:0000269|PubMed:9121430, ECO:0000269|PubMed:9566877
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 106
type MOD_RES
sequence X
description Phosphotyrosine => ECO:0000269|PubMed:8939605, ECO:0000269|PubMed:9121430, ECO:0000269|PubMed:9566877
source Swiss-Prot : SWS_FT_FI1

3) chain A
residue 718
type BINDING
sequence L
description 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
source Swiss-Prot : SWS_FT_FI2

4) chain A
residue 1016
type SITE
sequence Y
description Important for interaction with PIK3C2B
source Swiss-Prot : SWS_FT_FI6

5) chain A
residue 1016
type MOD_RES
sequence Y
description Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:23774213
source Swiss-Prot : SWS_FT_FI13

6) chain A
residue 869
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:23774213
source Swiss-Prot : SWS_FT_FI9

7) chain A
residue 745
type MOD_RES
sequence K
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
source Swiss-Prot : SWS_FT_FI8

8) chain A
residue 718-745
type prosite
sequence LGSGAFGTVYKGLWIPEGEKVKIPVAIK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGTVYkGlwipegekvkip......VAIK
source prosite : PS00107

9) chain A
residue 833-845
type prosite
sequence LVHRDLAARNVLV
description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHrDLAARNVLV
source prosite : PS00109

10) chain A
residue 929
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI15

11) chain A
residue 970
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144
source Swiss-Prot : SWS_FT_FI15

12) chain A
residue 757
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800
source Swiss-Prot : SWS_FT_FI16

13) chain A
residue 960
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33996800
source Swiss-Prot : SWS_FT_FI16

14) chain A
residue 716
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800
source Swiss-Prot : SWS_FT_FI14

15) chain A
residue 737
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800
source Swiss-Prot : SWS_FT_FI14

16) chain A
residue 754
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800
source Swiss-Prot : SWS_FT_FI14

17) chain A
residue 867
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:33996800
source Swiss-Prot : SWS_FT_FI14

18) chain A
residue 745
type BINDING
sequence K
description 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
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 790
type BINDING
sequence T
description 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
source Swiss-Prot : SWS_FT_FI4

20) chain A
residue 855
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI5


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