eF-site ID 1h8h-B
PDB Code 1h8h
Chain B

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Title Bovine mitochondrial F1-ATPase crystallised in the presence of 5mm AMPPNP
Classification HYDROLASE
Compound BOVINE MITOCHONDRIAL F1-ATPASE
Source ORGANISM_COMMON: CATTLE; ORGANISM_SCIENTIFIC: BOS TAURUS;
Sequence B:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS
LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL
LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR
EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI
INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA
DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH
ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS
RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI
SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM
KQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQG
QYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSH
VISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
Description


Functional site

1) chain B
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE MG B 601
source : AC2

2) chain B
residue 171
type
sequence R
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

3) chain B
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

4) chain B
residue 173
type
sequence T
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

5) chain B
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

6) chain B
residue 175
type
sequence K
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

7) chain B
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

8) chain B
residue 177
type
sequence S
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

9) chain B
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

10) chain B
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

11) chain B
residue 431
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

12) chain B
residue 432
type
sequence Q
description BINDING SITE FOR RESIDUE ATP B 600
source : AC8

13) chain B
residue 343
type
sequence I
description BINDING SITE FOR RESIDUE ATP F 600
source : BC2

14) chain B
residue 344
type
sequence S
description BINDING SITE FOR RESIDUE ATP F 600
source : BC2

15) chain B
residue 371
type
sequence V
description BINDING SITE FOR RESIDUE ATP F 600
source : BC2

16) chain B
residue 373
type
sequence R
description BINDING SITE FOR RESIDUE ATP F 600
source : BC2

17) chain B
residue 129
type
sequence V
description BINDING SITE FOR RESIDUE GOL B 701
source : BC3

18) chain B
residue 130
type
sequence G
description BINDING SITE FOR RESIDUE GOL B 701
source : BC3

19) chain B
residue 244
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 701
source : BC3

20) chain B
residue 248
type
sequence Y
description BINDING SITE FOR RESIDUE GOL B 701
source : BC3

21) chain B
residue 304
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 701
source : BC3

22) chain B
residue 430
type MOD_RES
sequence Q
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

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

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

25) chain B
residue 123
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

26) chain B
residue 141
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

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

28) chain B
residue 80
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

29) chain B
residue 83
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

30) chain B
residue 89
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

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

32) chain B
residue 118
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

33) chain B
residue 124
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

34) chain B
residue 187
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

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

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

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

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

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

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

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

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

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


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