eF-site ID 2h7v-ABCD
PDB Code 2h7v
Chain A, B, C, D

click to enlarge
Title Co-crystal structure of YpkA-Rac1
Classification SIGNALING PROTEIN
Compound Migration-inducing protein 5
Source Homo sapiens (Human) (YPKA_YERPS)
Sequence A:  GSKLMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTV
FDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTD
VSLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTK
LDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLE
CSALTQRGLKTVFDEAIRAVLC
B:  GSKLMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTV
FDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTD
VSLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTK
LDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLE
CSALTQRGLKTVFDEAIRAVLCP
C:  RITPKKLRELSDLLRTHLSSAATKQLDMGGVLSDLDTMLV
ALDKAEREGGVDKDQLKSFNSLILKTYRVIEDYVKGSNFM
LSIVEPSLQRIQKHLDQTHSFSDIGSLVRAHKHLETLLEV
LVTLSQQGQPVSSETYGFLNRLAEAKITLSQQLNTLQQQQ
ESAKAQLSILINRSGSWADVARQSLQRFDSTRPYTAIHRQ
MMAAHAAITLQEVSEFTDDMRNFTVDSIPLLIQLGRSSLM
DEHLVEQREKLRELTTIAERLNRLEREWM
D:  TPKKLRELSDLLRTHLSSAATKQLDMGGVLSDLDTMLVAL
DKAEREVDKDQLKSFNSLILKTYRVIEDYVNFMLSIVEPS
LQRIQKHLDQTHSFSDIGSLVRAHKHLETLLEVLVTLSQQ
GQPVSSETYGFLNRLAEAKITLSQQLNTLQQQQESAKAQL
SILINRSGSWADVARQSLQRFDSTRTAIHRQMMAAHAAIT
LQEVSEFTDDMRNFTVDSIPLLIQLGRSSLDEHLVEQREK
LRELTTIAERLNRLEREWM
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 B
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE MG B 201
source : AC2
4) chain B
residue 35
type
sequence T
description BINDING SITE FOR RESIDUE MG B 201
source : AC2
5) chain A
residue 11
type
sequence D
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
6) chain A
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
7) chain A
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
8) chain A
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
9) chain A
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
10) chain A
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
11) chain A
residue 18
type
sequence C
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
12) chain A
residue 28
type
sequence F
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
13) chain A
residue 33
type
sequence I
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
14) chain A
residue 116
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
15) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
16) chain A
residue 119
type
sequence L
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
17) chain A
residue 159
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
18) chain A
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GDP A 200
source : AC3
19) chain B
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
20) chain B
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
21) chain B
residue 15
type
sequence G
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
22) chain B
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
23) chain B
residue 17
type
sequence T
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
24) chain B
residue 18
type
sequence C
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
25) chain B
residue 28
type
sequence F
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
26) chain B
residue 33
type
sequence I
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
27) chain B
residue 116
type
sequence K
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
28) chain B
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
29) chain B
residue 119
type
sequence L
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
30) chain B
residue 158
type
sequence S
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
31) chain B
residue 159
type
sequence A
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
32) chain B
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GDP B 200
source : AC4
33) 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
34) 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
35) 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
36) chain B
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
37) chain B
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
38) chain B
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
39) 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
40) 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
41) chain B
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
42) chain B
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
43) 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_FI4
44) chain B
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_FI4
45) 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_FI9
46) chain B
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_FI9
47) 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_FI10
48) chain B
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_FI10
49) 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_FI3
50) chain B
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_FI3
51) chain A
residue 71
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:10617634
source Swiss-Prot : SWS_FT_FI5
52) chain B
residue 71
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:10617634
source Swiss-Prot : SWS_FT_FI5
53) 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_FI7
54) chain B
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_FI7
55) 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_FI8
56) chain B
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_FI8

Display surface

Download
Links