eF-site ID 3h0l-V
PDB Code 3h0l
Chain V

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Title Structure of trna-dependent amidotransferase gatcab from aquifex aeolicus
Classification LIGASE
Compound Glutamyl-tRNA(Gln) amidotransferase subunit A
Source Aquifex aeolicus (GATC_AQUAE)
Sequence V:  MLWKKSLSELRELLKRGEVSPKEVVESFYDRYNQTEEKVK
AYITPLYGKALKQAESLKERELPLFGIPIAVKDNILVEGE
KTTCASKILENFVAPYDATVIERLKKAGALIVGKTNLDEF
AMGSSTEYSAFFPTKNPWDLERVPGGSSGGSAASVAVLSA
PVSLGSDTGGSIRQPASFCGVIGIKPTYGRVSRYGLVAFA
SSLDQIGVFGRRTEDVALVLEVISGWDEKDSTSAKVPVPE
WSEEVKKEVKGLKIGLPKEFFEYELQPQVKEAFENFIKEL
EKEGFEIKEVSLPHVKYSIPTYYIIAPSEASSNLARYDGV
RYGYRAKEYKDIFEMYARTRDEGFGPEVKRRIMLGTFALS
AGYYDAYYLKAQKVRRLITNDFLKAFEEVDVIASPTTPTL
PFKFGERLENPIEMYLSDILTVPANLAGLPAISIPIAWKD
GLPVGGQLIGKHWDETTLLQISYLWEQKFKHYEKIPLT
Description


Functional site

1) chain V
residue 121
type
sequence A
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

2) chain V
residue 123
type
sequence G
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

3) chain V
residue 169
type
sequence G
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

4) chain V
residue 170
type
sequence G
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

5) chain V
residue 171
type
sequence S
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

6) chain V
residue 199
type
sequence F
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

7) chain V
residue 302
type
sequence Y
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

8) chain V
residue 351
type
sequence R
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

9) chain V
residue 418
type
sequence D
description BINDING SITE FOR RESIDUE ASN V 908
source : DC5

10) chain V
residue 72
type ACT_SITE
sequence K
description Charge relay system => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

11) chain V
residue 147
type ACT_SITE
sequence S
description Charge relay system => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

12) chain V
residue 171
type ACT_SITE
sequence S
description Acyl-ester intermediate => ECO:0000250
source Swiss-Prot : SWS_FT_FI2


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