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

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Title BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN
Classification HYDROLASE/ANTIBIOTIC
Compound BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA
Source ORGANISM_COMMON: CATTLE; 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 162
type
sequence K
description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

2) chain E
residue 188
type
sequence E
description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE.
source : CAT

3) chain E
residue 155
type
sequence F
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

4) chain E
residue 315
type
sequence D
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

5) chain E
residue 317
type
sequence L
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

6) chain E
residue 332
type
sequence T
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

7) chain E
residue 352
type
sequence D
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

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

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

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

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

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

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

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

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

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

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

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

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

24) 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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