eF-site ID 6jxj-A
PDB Code 6jxj
Chain A

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Title Rb+-bound E2-AlF state of the gastric proton pump (Tyr799Trp)
Classification MEMBRANE PROTEIN
Compound Potassium-transporting ATPase alpha chain 1
Source (ATP4B_PIG)
Sequence A:  GMEINDHQLSVAELEQKYQTSATKGLSASLAAELLLRDGP
NALRPPRGTPEYVKFARQLAGGLQCLMWVAAAICLIAFAI
QASEGDLTTDDNLYLALALIAVVVVTGCFGYYQEFKSTNI
IASFKNLVPQQATVIRDGDKFQINADQLVVGDLVEMKGGD
RVPADIRILQAQGCKVDNSSLTGESEPQTRSPECTHESPL
ETRNIAFFSTMCLEGTAQGLVVNTGDRTIIGRIASLASGV
ENEKTPIAIEIEHFVDIIAGLAILFGATFFIVAMCIGYTF
LRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRLASKNCV
VKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHI
HSADTTEDQSGQTFDQSSETWRALCRVLTLCNRAAFKSGQ
DAVPVPKRIVIGDASETALLKFSELTLGNAMGYRERFPKV
CEIPFNSTNKFQLSIHTLEDPRDPRHVLVMKGAPERVLER
CSSILIKGQELPLDEQWREAFQTAYLSLGGLGERVLGFCQ
LYLSEKDYPPGYAFDVEAMNFPTSGLCFAGLVSMIDPPRA
TVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEG
SETVEDIAARLRVPVDQVNRKDARACVINGMQLKDMDPSE
LVEALRTHPEMVFARTSPQQKLVIVESCQRLGAIVAVTGD
GVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFAS
IVTGVEQGRLIFDNLKKSIAYTLTKNIPELTPWLIYITVS
VPLPLGCITILFIELCTDIFPSVSLAYEKAESDIMHLRPR
NPKRDRLVNEPLAAYSYFQIGAIQSFAGFTDYFTAMAQEG
WFPLLCVGLRPQWENHHLQDLQDSYGQEWTFGQRLYQQYT
CYTVFFISIEMCQIADVLIRKTRRLSAFQQGFFRNRILVI
AIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFSL
LIFVYDEIRKLGVRCCPGSWWDQELYY
Description


Functional site

1) chain A
residue 338
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI5

2) chain A
residue 339
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI5

3) chain A
residue 341
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI5

4) chain A
residue 343
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI5

5) chain A
residue 795
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI5

6) chain A
residue 820
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:31436534, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI5

7) chain A
residue 996-1016
type TRANSMEM
sequence QWWLVPMPFSLLIFVYDEIRK
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

8) chain A
residue 141-161
type TRANSMEM
sequence LALALIAVVVVTGCFGYYQEF
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

9) chain A
residue 298-317
type TRANSMEM
sequence EHFVDIIAGLAILFGATFFI
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

10) chain A
residue 330-347
type TRANSMEM
sequence MVFFMAIVVAYVPEGLLA
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

11) chain A
residue 782-801
type TRANSMEM
sequence KKSIAYTLTKNIPELTPWLI
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 812-832
type TRANSMEM
sequence GCITILFIELCTDIFPSVSLA
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 853-875
type TRANSMEM
sequence LVNEPLAAYSYFQIGAIQSFAGF
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 928-947
type TRANSMEM
sequence YTVFFISIEMCQIADVLIRK
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 962-980
type TRANSMEM
sequence RILVIAIVFQVCIGCFLCY
description Helical; Signal-anchor for type II membrane protein => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 318-329
type TOPO_DOM
sequence VAMCIGYTFLRA
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

17) chain A
residue 802-811
type TOPO_DOM
sequence YITVSVPLPL
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

18) chain A
residue 876-927
type TOPO_DOM
sequence TDYFTAMAQEGWFPLLCVGLRPQWENHHLQDLQDSYGQEW
TFGQRLYQQYTC
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 981-995
type TOPO_DOM
sequence CPGMPNIFNFMPIRF
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 385
type ACT_SITE
sequence D
description 4-aspartylphosphate intermediate => ECO:0000269|PubMed:1720615
source Swiss-Prot : SWS_FT_FI4

21) chain A
residue 385
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI6

22) chain A
residue 387
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI6

23) chain A
residue 726
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU, ECO:0007744|PDB:6JXH
source Swiss-Prot : SWS_FT_FI6

24) chain A
residue 730
type BINDING
sequence D
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

25) chain A
residue 461
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q6PIE5
source Swiss-Prot : SWS_FT_FI8

26) chain A
residue 599
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P50993
source Swiss-Prot : SWS_FT_FI9

27) chain A
residue 838
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P09626
source Swiss-Prot : SWS_FT_FI10

28) chain A
residue 952
type MOD_RES
sequence S
description Phosphoserine; by PKA => ECO:0000250
source Swiss-Prot : SWS_FT_FI11

29) chain A
residue 385-391
type prosite
sequence DKTGTLT
description ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
source prosite : PS00154


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