eF-site ID 1h8e-E
PDB Code 1h8e
Chain E

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Title (ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied)
Classification HYDROLASE
Compound BOVINE MITOCHONDRIAL F1-ATPASE
Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS;
Sequence E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE
VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP
ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMEQ
EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELI
NNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKD
ATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD
VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMG
TMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLD
ATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDV
ARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKI
QRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYD
HLPEQAFYMVGPIE
Description


Functional site

1) chain E
residue 159
type
sequence G
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

2) chain E
residue 160
type
sequence V
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

3) chain E
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

4) chain E
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

5) chain E
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

6) chain E
residue 164
type
sequence V
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

7) chain E
residue 345
type
sequence Y
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

8) chain E
residue 421
type
sequence A
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

9) chain E
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE MG E 601
source : BC7

10) chain E
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE SO4 E 630
source : BC8

11) chain E
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE SO4 E 630
source : BC8

12) chain E
residue 189
type
sequence R
description BINDING SITE FOR RESIDUE SO4 E 630
source : BC8

13) chain E
residue 260
type
sequence R
description BINDING SITE FOR RESIDUE SO4 E 630
source : BC8

14) chain E
residue 311
type
sequence Y
description BINDING SITE FOR RESIDUE SO4 E 630
source : BC8

15) chain E
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA2

16) chain E
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA2

17) chain E
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA2

18) chain E
residue 74
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

19) chain E
residue 111
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

20) chain E
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

21) chain E
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

22) chain E
residue 148
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

23) chain E
residue 376
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

24) chain E
residue 262
type MOD_RES
sequence T
description Phosphoserine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI5

25) chain E
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

26) chain E
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

27) chain E
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

28) chain E
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

29) chain E
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9


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