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

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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 A:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG
LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP
VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP
RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI
AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK
RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR
DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV
FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI
PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA
QTRAMKQVAGTMKLELAQYREVAAFLDAATQQLLSRGVRL
TELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKF
ENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNF
LAGFEA
Description


Functional site

1) chain A
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

2) chain A
residue 173
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

3) chain A
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

4) chain A
residue 175
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

5) chain A
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

6) chain A
residue 177
type
sequence S
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

7) chain A
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

8) chain A
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

9) chain A
residue 432
type
sequence Q
description BINDING SITE FOR RESIDUE ADP A 600
source : AC1

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

11) chain A
residue 244
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 602
source : AC3

12) chain A
residue 245
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 602
source : AC3

13) chain A
residue 248
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 602
source : AC3

14) chain A
residue 304
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 602
source : AC3

15) chain A
residue 373
type
sequence R
description BINDING SITE FOR RESIDUE ADP E 600
source : BC6

16) chain A
residue 373
type
sequence R
description BINDING SITE FOR RESIDUE SO4 E 630
source : BC8

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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