eF-site ID 5fr1-AB
PDB Code 5fr1
Chain A, B

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Title Double acetylated RhoGDI-alpha in complex with RhoA-GDP
Classification SIGNALING PROTEIN
Compound TRANSFORMING PROTEIN RHOA
Source (GDIR1_BOVIN)
Sequence A:  IRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYV
ADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMC
FSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRN
DEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKT
KDGVREVFEMATRAALQASGCLVL
B:  NYKPPAQKSIQEIQELDKDDESLRKYKEALLVPNVVVTRL
TLVCSTAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKIS
FRVNREIVSGMXYIQHTYRKGVKIDXTDYMVGSYGPRAEE
YEFLTPMEEAPKGMLARGSYNIKSRFTDDDRTDHLSWEWN
LTIKKEW
Description


Functional site

1) chain A
residue 13
type
sequence D
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

2) chain A
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

3) chain A
residue 16
type
sequence C
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

4) chain A
residue 17
type
sequence G
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

5) chain A
residue 18
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

6) chain A
residue 19
type
sequence T
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

7) chain A
residue 20
type
sequence C
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

8) chain A
residue 30
type
sequence F
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

9) chain A
residue 35
type
sequence V
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

10) chain A
residue 118
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

11) chain A
residue 120
type
sequence D
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

12) chain A
residue 121
type
sequence L
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

13) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

14) chain A
residue 161
type
sequence A
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

15) chain A
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE GDP A 1194
source : AC1

16) chain A
residue 19
type
sequence T
description BINDING SITE FOR RESIDUE MG A 1195
source : AC2

17) chain A
residue 37
type
sequence T
description BINDING SITE FOR RESIDUE MG A 1195
source : AC2

18) chain A
residue 43
type
sequence V
description BINDING SITE FOR RESIDUE MG A 1196
source : AC3

19) chain A
residue 45
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1196
source : AC3

20) chain B
residue 117
type
sequence R
description BINDING SITE FOR RESIDUE MG B 1203
source : AC4

21) chain B
residue 118
type
sequence V
description BINDING SITE FOR RESIDUE MG B 1203
source : AC4

22) chain B
residue 152
type
sequence R
description BINDING SITE FOR RESIDUE MG B 1203
source : AC4

23) chain B
residue 154
type
sequence E
description BINDING SITE FOR RESIDUE MG B 1203
source : AC4

24) chain B
residue 105
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI6

25) chain B
residue 127
type MOD_RES
sequence X
description N6-acetyllysine => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI6

26) chain B
residue 178
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI6

27) chain A
residue 34
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_FI12

28) chain A
residue 135
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23871831
source Swiss-Prot : SWS_FT_FI14

29) chain A
residue 117
type MOD_RES
sequence N
description N-acetylalanine => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 34
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q99PT1
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 59
type MOD_RES
sequence D
description Phosphoserine => ECO:0000250|UniProtKB:Q99PT1
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 160
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q99PT1
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 43
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q99PT1
source Swiss-Prot : SWS_FT_FI3

34) chain B
residue 47
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI4

35) chain B
residue 101
type MOD_RES
sequence S
description Phosphoserine; by PKA => ECO:0000255
source Swiss-Prot : SWS_FT_FI5

36) chain A
residue 190
type LIPID
sequence C
description S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P61585
source Swiss-Prot : SWS_FT_FI11

37) chain B
residue 115
type MOD_RES
sequence S
description Phosphoserine; by PKC => ECO:0000255
source Swiss-Prot : SWS_FT_FI7

38) chain B
residue 141
type MOD_RES
sequence X
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99PT1
source Swiss-Prot : SWS_FT_FI8

39) chain B
residue 138
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI9

40) chain B
residue 141
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P52565
source Swiss-Prot : SWS_FT_FI9

41) chain A
residue 37
type CARBOHYD
sequence T
description (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate => ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059
source Swiss-Prot : SWS_FT_FI13


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