eF-site ID 1a0g-A
PDB Code 1a0g
Chain A

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Title L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE
Classification TRANSFERASE
Compound D-AMINO ACID AMINOTRANSFERASE
Source Bacillus sp. (strain YM-1) (DAAA_BACYM)
Sequence A:  GYTLWNDQIVKDEEVKIDKEDRGYQFGDGVYEVVKVYNGE
MFTVNEHIDRLYASAEKIRITIPYTKDKFHQLLHELVEKN
ELNTGHIYFQVTRGTSPRAHQFPENTVKPVIIGYTKENPR
PLENLEKGVKATFVEDIRWLRCDIKSLNLLGAVLAKQEAH
EKGCYEAILHRNNTVTEGSSSNVFGIKDGILYTHPANNMI
AKGITRDVVIACANEINMPVKEIPFTTHEALKMDELFVTS
TTSEITPVIEIDGKLIRDGKVGEWTRKLQKQFETKIPKPL
Description


Functional site

1) chain A
residue 145
type
sequence K
description AN ACTIVE SITE FOR SUBUNIT A.
source : ASA

2) chain A
residue 31
type
sequence Y
description AN ACTIVE SITE FOR SUBUNIT A.
source : ASA

3) chain A
residue 177
type
sequence E
description AN ACTIVE SITE FOR SUBUNIT A.
source : ASA

4) chain A
residue 98
type
sequence R
description AN ACTIVE SITE FOR SUBUNIT B.
source : ASB

5) chain A
residue 31
type
sequence Y
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

6) chain A
residue 50
type
sequence R
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

7) chain A
residue 145
type
sequence K
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

8) chain A
residue 177
type
sequence E
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

9) chain A
residue 180
type
sequence S
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

10) chain A
residue 181
type
sequence S
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

11) chain A
residue 182
type
sequence N
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

12) chain A
residue 201
type
sequence A
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

13) chain A
residue 203
type
sequence G
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

14) chain A
residue 204
type
sequence I
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

15) chain A
residue 205
type
sequence T
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

16) chain A
residue 240
type
sequence S
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

17) chain A
residue 241
type
sequence T
description BINDING SITE FOR RESIDUE PMP A 285
source : AC1

18) chain A
residue 32
type catalytic
sequence E
description 66
source MCSA : MCSA1

19) chain A
residue 146
type catalytic
sequence S
description 66
source MCSA : MCSA1

20) chain A
residue 178
type catalytic
sequence G
description 66
source MCSA : MCSA1

21) chain A
residue 202
type catalytic
sequence K
description 66
source MCSA : MCSA1

22) chain A
residue 146
type ACT_SITE
sequence S
description Proton acceptor => ECO:0000269|PubMed:7626635
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 32
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9538014
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 51
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:9538014
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 99
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:9538014
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 101
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9538014
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 178
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:9538014
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 146
type MOD_RES
sequence S
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7626635
source Swiss-Prot : SWS_FT_FI3


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