eF-site ID 1w0j-E
PDB Code 1w0j
Chain E

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Title Beryllium fluoride inhibited bovine F1-ATPase
Classification HYDROLASE
Compound ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, MITOCHONDRIAL PRECURSOR
Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS;
Sequence E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE
VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP
ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV
EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME
LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG
QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD
MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH
LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY
DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE
YDHLPEQAFYMVGPIEEAVAKADKLA
Description


Functional site

1) chain E
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE PO4 E 1475
source : AC1

2) chain E
residue 159
type
sequence G
description BINDING SITE FOR RESIDUE PO4 E 1475
source : AC1

3) chain E
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE PO4 E 1475
source : AC1

4) chain E
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE PO4 E 1475
source : AC1

5) chain E
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE PO4 E 1475
source : AC1

6) chain E
residue 356
type
sequence R
description BINDING SITE FOR RESIDUE ADP B 1511
source : AC8

7) chain E
residue 359
type
sequence D
description BINDING SITE FOR RESIDUE ADP B 1511
source : AC8

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

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

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

11) chain E
residue 157
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

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

13) chain E
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

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

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

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

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

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

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

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

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

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

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

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


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