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

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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 A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS
LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL
LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR
EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI
INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA
DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH
ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS
RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI
SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM
KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR
LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK
FENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTN
FLAGFEA
Description


Functional site

1) chain A
residue 175
type
sequence K
description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

2) chain A
residue 373
type
sequence R
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 A
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE MG A 601
source : AC1

4) chain A
residue 170
type
sequence D
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

5) chain A
residue 171
type
sequence R
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

6) chain A
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

7) chain A
residue 173
type
sequence T
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

8) chain A
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

9) chain A
residue 175
type
sequence K
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

10) chain A
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

11) chain A
residue 177
type
sequence S
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

12) chain A
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

13) chain A
residue 362
type
sequence R
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

14) chain A
residue 363
type
sequence P
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

15) chain A
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

16) chain A
residue 432
type
sequence Q
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

17) chain A
residue 331
type
sequence A
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

18) chain A
residue 332
type
sequence G
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

19) chain A
residue 333
type
sequence D
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

20) chain A
residue 334
type
sequence V
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

21) chain A
residue 335
type
sequence S
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

22) chain A
residue 349
type
sequence Q
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

23) chain A
residue 351
type
sequence F
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

24) chain A
residue 369
type
sequence L
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

25) chain A
residue 363-372
type prosite
sequence PAINVGLSVS
description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS
source prosite : PS00152

26) chain A
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

27) chain A
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

28) chain A
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

29) chain A
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

30) chain A
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

31) chain A
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

32) chain A
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

33) chain A
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

34) chain A
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

35) chain A
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

36) chain A
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

37) chain A
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

38) chain A
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9


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