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

click to enlarge
Title COMPLEX OF RAN WITH IMPORTIN BETA
Classification cell cycle,translation
Compound GTP-binding nuclear protein RAN
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  VQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVH
PLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAII
MFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKD
RKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKL
IGDPNLEFV
Description


Functional site
1) chain A
residue 24
type
sequence T
description BINDING SITE FOR RESIDUE MG A 251
source : AC1
2) chain A
residue 40
type
sequence V
description BINDING SITE FOR RESIDUE MG A 251
source : AC1
3) chain A
residue 42
type
sequence T
description BINDING SITE FOR RESIDUE MG A 251
source : AC1
4) chain A
residue 19
type
sequence G
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
5) chain A
residue 20
type
sequence G
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
6) chain A
residue 21
type
sequence T
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
7) chain A
residue 22
type
sequence G
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
8) chain A
residue 23
type
sequence K
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
9) chain A
residue 24
type
sequence T
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
10) chain A
residue 25
type
sequence T
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
11) chain A
residue 35
type
sequence F
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
12) chain A
residue 36
type
sequence E
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
13) chain A
residue 37
type
sequence K
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
14) chain A
residue 38
type
sequence K
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
15) chain A
residue 39
type
sequence Y
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
16) chain A
residue 41
type
sequence A
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
17) chain A
residue 42
type
sequence T
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
18) chain A
residue 68
type
sequence G
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
19) chain A
residue 69
type
sequence Q
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
20) chain A
residue 122
type
sequence N
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
21) chain A
residue 123
type
sequence K
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
22) chain A
residue 125
type
sequence D
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
23) chain A
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
24) chain A
residue 150
type
sequence S
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
25) chain A
residue 151
type
sequence A
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
26) chain A
residue 152
type
sequence K
description BINDING SITE FOR RESIDUE GNP A 250
source : AC3
27) chain A
residue 69
type SITE
sequence Q
description Essential for GTP hydrolysis => ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:8636225
source Swiss-Prot : SWS_FT_FI6
28) chain A
residue 24
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI8
29) chain A
residue 37
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:31075303
source Swiss-Prot : SWS_FT_FI9
30) chain A
residue 60
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI10
31) chain A
residue 99
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI10
32) chain A
residue 71
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI11
33) chain A
residue 134
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:29040603
source Swiss-Prot : SWS_FT_FI12
34) chain A
residue 159
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62827
source Swiss-Prot : SWS_FT_FI13
35) chain A
residue 71
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
source Swiss-Prot : SWS_FT_FI14
36) chain A
residue 152
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI15
37) chain A
residue 122
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, ECO:0007744|PDB:3CH5, ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CJ2, ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW
source Swiss-Prot : SWS_FT_FI4
38) chain A
residue 150
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1K5G, ECO:0007744|PDB:3CH5, ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CJ2, ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5CLQ, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW
source Swiss-Prot : SWS_FT_FI5

Display surface

Download
Links