eF-site ID 1e96-AB
PDB Code 1e96
Chain A, B

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Title Structure of the Rac/p67phox complex
Classification SIGNALING PROTEIN
Compound RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1
Source (NCF2_HUMAN)
Sequence A:  PQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNY
SANVMVDGKPVNLGLWDTAGLEDYDRLRPLSYPQTDVFLI
CFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSAL
TQRGLKTVFDEAIRAVLC
B:  SLVEAISLWNEGVLAADKKDWKGALDAFSAVQDPHSRICF
NIGCMYTILKNMTEAEKAFTRSINRDKHLAVAYFQRGMLY
YQTEKYDLAIKDLKEALIQLRGNQLIDYKILGLQFKLFAC
EVLYNIAFMYAKKEEWKKAEEQLALATSMKSEPRHSKIDK
AMECVWKQKLYEPVVIPVGKLFRPN
Description


Functional site

1) chain A
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE MG A 201
source : AC1

2) chain A
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE MG A 201
source : AC1

3) chain A
residue 57
type
sequence D
description BINDING SITE FOR RESIDUE MG A 201
source : AC1

4) chain A
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

5) chain A
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

6) chain A
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

7) chain A
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

8) chain A
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

9) chain A
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

10) chain A
residue 18
type
sequence C
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

11) chain A
residue 28
type
sequence F
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

12) chain A
residue 29
type
sequence P
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

13) chain A
residue 30
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

14) chain A
residue 32
type
sequence Y
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

15) chain A
residue 34
type
sequence P
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

16) chain A
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

17) chain A
residue 60
type
sequence G
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

18) chain A
residue 116
type
sequence K
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

19) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

20) chain A
residue 119
type
sequence L
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

21) chain A
residue 158
type
sequence S
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

22) chain A
residue 159
type
sequence A
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

23) chain A
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GTP A 200
source : AC2

24) chain A
residue 13
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 30
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 60
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 116
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR, ECO:0007744|PDB:5HZH
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 159
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:11090627, ECO:0007744|PDB:1E96, ECO:0007744|PDB:2WKP, ECO:0007744|PDB:2WKQ, ECO:0007744|PDB:2WKR, ECO:0007744|PDB:5HZH
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 32
type CARBOHYD
sequence Y
description (Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate => ECO:0000269|PubMed:24141704
source Swiss-Prot : SWS_FT_FI11

30) chain A
residue 35
type CARBOHYD
sequence T
description (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB, and by P.sordellii toxin TcsL; alternate => ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059
source Swiss-Prot : SWS_FT_FI12

31) chain A
residue 71
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:10617634
source Swiss-Prot : SWS_FT_FI3

32) chain A
residue 147
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18093184
source Swiss-Prot : SWS_FT_FI6

33) chain A
residue 166
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23512198
source Swiss-Prot : SWS_FT_FI7

34) chain A
residue 32
type MOD_RES
sequence Y
description (Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate => ECO:0000269|PubMed:19362538
source Swiss-Prot : SWS_FT_FI8

35) chain A
residue 35
type MOD_RES
sequence T
description (Microbial infection) O-AMP-threonine; by Vibrio VopS => ECO:0000269|PubMed:19039103
source Swiss-Prot : SWS_FT_FI9


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