eF-site ID 3oo2-AB
PDB Code 3oo2
Chain A, B

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Title 2.37 Angstrom resolution crystal structure of an alanine racemase (alr) from Staphylococcus aureus subsp. aureus COL
Classification ISOMERASE
Compound Alanine racemase 1
Source Staphylococcus aureus (strain COL) (ALR1_STAAC)
Sequence A:  SDKYYRSAYMNVDLNAVASNFKVFSTLHPNKTVMAVVKAN
AYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAK
ILVLGVLPAKDIDKAIQHRVALTVPSKQWLKEAIKNISGE
QEKKLWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLV
FEGVFTHFACADEPGDMTTEQYQRFKDMVNEAIKPEYIHC
QNSAGSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKVHL
KPSVQLIANVVQTKTLQAGESVSYGYTATDPTTIALLPIG
YADGYLRIMQGSFVNVNGHQCEVIGRVCMDQTIVKVPDQV
KAGDSVILIDNHRESPQSVEVVAEKQHTINYEVLCNLSRR
LPRIYHDGDQRFVTNELLK
B:  SDKYYRSAYMNVDLNAVASNFKVFSTLHPNKTVMAVVKAN
AYGLGSVKVARHLMENGATFFAVATLDEAIELRMHGITAK
ILVLGVLPAKDIDKAIQHRVALTVPSKQWLKEAIKNISKK
LWLHIKLDTGMGRLGIKDTKTYQEVIEIIQQYEQLVFEGV
FTHFACADEPGDMTTEQYQRFKDMVNEAIKPEYIHCQNSA
GSLLMDCQFCNAIRPGISLYGYYPSEYVQQKVKVHLKPSV
QLIANVVQTKTLQADPTTIALLPIGYADGYLRIMQGSFVN
VNGHQCEVIGRVCMDQTIVKVPDQVKAGDSVILIDNHRES
PQSVEVVAEKQHTINYEVLCNLSRRLPRIYHDGDQRFVTN
ELLK
Description


Functional site

1) chain A
residue 154
type
sequence I
description BINDING SITE FOR RESIDUE NA A 383
source : AC1

2) chain A
residue 157
type
sequence Y
description BINDING SITE FOR RESIDUE NA A 383
source : AC1

3) chain A
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE NA A 383
source : AC1

4) chain A
residue 170
type
sequence A
description BINDING SITE FOR RESIDUE BME A 384
source : AC2

5) chain A
residue 171
type
sequence C
description BINDING SITE FOR RESIDUE BME A 384
source : AC2

6) chain A
residue 173
type
sequence D
description BINDING SITE FOR RESIDUE BME A 384
source : AC2

7) chain A
residue 174
type
sequence E
description BINDING SITE FOR RESIDUE BME A 384
source : AC2

8) chain B
residue 309
type
sequence R
description BINDING SITE FOR RESIDUE BME A 384
source : AC2

9) chain A
residue 311
type
sequence C
description BINDING SITE FOR RESIDUE BME A 385
source : AC3

10) chain B
residue 138
type
sequence R
description BINDING SITE FOR RESIDUE BME A 385
source : AC3

11) chain A
residue 43
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 A 386
source : AC4

12) chain A
residue 203
type
sequence N
description BINDING SITE FOR RESIDUE PO4 A 386
source : AC4

13) chain A
residue 204
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 386
source : AC4

14) chain A
residue 221
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 386
source : AC4

15) chain A
residue 222
type
sequence I
description BINDING SITE FOR RESIDUE PO4 A 386
source : AC4

16) chain A
residue 354
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 A 386
source : AC4

17) chain B
residue 154
type
sequence I
description BINDING SITE FOR RESIDUE NA B 383
source : AC5

18) chain B
residue 157
type
sequence Y
description BINDING SITE FOR RESIDUE NA B 383
source : AC5

19) chain B
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE NA B 383
source : AC5

20) chain B
residue 309
type
sequence R
description BINDING SITE FOR RESIDUE BME B 384
source : AC6

21) chain B
residue 311
type
sequence C
description BINDING SITE FOR RESIDUE BME B 384
source : AC6

22) chain B
residue 43
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 B 385
source : AC7

23) chain B
residue 203
type
sequence N
description BINDING SITE FOR RESIDUE PO4 B 385
source : AC7

24) chain B
residue 204
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 385
source : AC7

25) chain B
residue 221
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 385
source : AC7

26) chain B
residue 222
type
sequence I
description BINDING SITE FOR RESIDUE PO4 B 385
source : AC7

27) chain B
residue 354
type
sequence Y
description BINDING SITE FOR RESIDUE PO4 B 385
source : AC7

28) chain A
residue 36-46
type prosite
sequence AVVKANAYGLG
description ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGLG
source prosite : PS00395

29) chain A
residue 39
type ACT_SITE
sequence K
description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 39
type ACT_SITE
sequence K
description Proton acceptor; specific for D-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 265
type ACT_SITE
sequence Y
description Proton acceptor; specific for L-alanine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 138
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 312
type BINDING
sequence M
description BINDING => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI3

34) chain B
residue 138
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI3

35) chain B
residue 312
type BINDING
sequence M
description BINDING => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 39
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI4

37) chain B
residue 39
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01201
source Swiss-Prot : SWS_FT_FI4


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