eF-site ID 1nwc-AB
PDB Code 1nwc
Chain A, B

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Title Crystal Structure of Aspartate-Semialdehyde Dehydrogenase from Haemophilus influenzae
Classification OXIDOREDUCTASE
Compound Aspartate-semialdehyde dehydrogenase
Source null (DHAS_HAEIN)
Sequence A:  MKNVGFIGWRGMVGSVLMDRMSQENDFENLNPVFFTTSQL
KSAFDIEELKKLDIIVTCQGGDYTNEVYPKLKATGWDGYW
VDAASALRMKDDAIIVLDPVNQHVISEGLKKGIKTFVGGN
CTVSLMLMAIGGLFEKDLVEWISVATYQAASGAGAKNMRE
LLSQMGLLEQAVSSELKDPASSILDIERKVTAKMRADNFP
TDNFGAALGGSLIPWIDKLLPETGQTKEEWKGYAETNKIL
GLSDNPIPVDGLCVRIGALRCHSQAFTIKLKKDLPLEEIE
QIIASHNEWVKVIPNDKEITLRELTPAKVTGTLSVPVGRL
RKLAMGPEYLAAFTVGDQLLWGAAEPVRRILKQLVA
B:  MKNVGFIGWRGMVGSVLMDRMSQENDFENLNPVFFTTSQL
KSAFDIEELKKLDIIVTCQGGDYTNEVYPKLKATGWDGYW
VDAASALRMKDDAIIVLDPVNQHVISEGLKKGIKTFVGGN
CTVSLMLMAIGGLFEKDLVEWISVATYQAASGAGAKNMRE
LLSQMGLLEQAVSSELKDPASSILDIERKVTAKMRADNFP
TDNFGAALGGSLIPWIDKLLPETGQTKEEWKGYAETNKIL
GLSDNPIPVDGLCVRIGALRCHSQAFTIKLKKDLPLEEIE
QIIASHNEWVKVIPNDKEITLRELTPAKVTGTLSVPVGRL
RKLAMGPEYLAAFTVGDQLLWGAAEPVRRILKQLVA
Description


Functional site

1) chain A
residue 136
type ACT_SITE
sequence C
description Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 136
type ACT_SITE
sequence C
description Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI1

3) chain B
residue 277
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000269|PubMed:14559965
source Swiss-Prot : SWS_FT_FI2

4) chain A
residue 277
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000269|PubMed:14559965
source Swiss-Prot : SWS_FT_FI2

5) chain A
residue 10
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

6) chain A
residue 37
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

7) chain B
residue 353
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

8) chain A
residue 74
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

9) chain A
residue 166
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

10) chain A
residue 353
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

11) chain B
residue 10
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

12) chain B
residue 37
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

13) chain B
residue 74
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

14) chain B
residue 166
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:15272161
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 103
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14559965
source Swiss-Prot : SWS_FT_FI4

16) chain A
residue 246
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14559965
source Swiss-Prot : SWS_FT_FI4

17) chain B
residue 103
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:14559965
source Swiss-Prot : SWS_FT_FI4

18) chain B
residue 246
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:14559965
source Swiss-Prot : SWS_FT_FI4

19) chain A
residue 163
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:15272161
source Swiss-Prot : SWS_FT_FI5

20) chain A
residue 243
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:15272161
source Swiss-Prot : SWS_FT_FI5

21) chain A
residue 270
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:15272161
source Swiss-Prot : SWS_FT_FI5

22) chain B
residue 243
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:15272161
source Swiss-Prot : SWS_FT_FI5

23) chain B
residue 270
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:15272161
source Swiss-Prot : SWS_FT_FI5

24) chain B
residue 163
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:15272161
source Swiss-Prot : SWS_FT_FI5

25) chain A
residue 264-278
type prosite
sequence VDGLCVRIGALRCHS
description ASD Aspartate-semialdehyde dehydrogenase signature. VDglCvRIgalrCHS
source prosite : PS01103


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