eF-site ID 5x9h-B
PDB Code 5x9h
Chain B

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Title Crystal structure of the Mg2+ channel MgtE in complex with ATP
Classification METAL TRANSPORT
Compound Magnesium transporter MgtE
Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (MGTE_THET8)
Sequence B:  EVLEEIHPQDLLALWDELKGEHRYVVLTLLPKAKAAEVLS
HLSPEEQAEYLKTLPPWRLREILEELSLDDLADALQAVRK
EDPAYFQRLKDLLDPRTRAEVEALARYEEDEAGGLMTPEY
VAVREGMTVEEVLRFLRRAAPDAETIYYIYVVDEKGRLKG
VLSLRDLIVADPRTRVAEIMNPKVVYVRTDTDQEEVARLM
ADYDFTVLPVVDEEGRLVGIVTVDDVLDVLEAEATEDIHK
LGAVDVPDLVYSEAGPVALWLARVRWLVILILTGMVTSSI
LQGFESVLEAVTALAFYVPVLLGTGGNTGNQSATLIIRAL
ATRDLDLRDWRRVFLKEMGVGLLLGLTLSFLLVGKVYWDG
HPLLLPVVGVSLVLIVFFANLVGAMLPFLLRRLGVDPALV
SNPLVATLSDVTGLLIYLSVARLLLE
Description


Functional site
1) chain B
residue 166
type
sequence E
description binding site for residue ATP A 501
source : AC1
2) chain B
residue 169
type
sequence Y
description binding site for residue ATP A 501
source : AC1
3) chain B
residue 250
type
sequence D
description binding site for residue MG A 506
source : AC5
4) chain B
residue 226
type
sequence D
description binding site for residue MG A 508
source : AC7
5) chain B
residue 59
type
sequence E
description binding site for residue MG A 509
source : AC8
6) chain B
residue 170
type
sequence Y
description binding site for residue ATP B 501
source : AC9
7) chain B
residue 183
type
sequence V
description binding site for residue ATP B 501
source : AC9
8) chain B
residue 185
type
sequence S
description binding site for residue ATP B 501
source : AC9
9) chain B
residue 187
type
sequence R
description binding site for residue ATP B 501
source : AC9
10) chain B
residue 188
type
sequence D
description binding site for residue ATP B 501
source : AC9
11) chain B
residue 203
type
sequence N
description binding site for residue ATP B 501
source : AC9
12) chain B
residue 205
type
sequence K
description binding site for residue ATP B 501
source : AC9
13) chain B
residue 206
type
sequence V
description binding site for residue ATP B 501
source : AC9
14) chain B
residue 207
type
sequence V
description binding site for residue ATP B 501
source : AC9
15) chain B
residue 227
type
sequence F
description binding site for residue ATP B 501
source : AC9
16) chain B
residue 223
type
sequence A
description binding site for residue MG B 502
source : AD1
17) chain B
residue 224
type
sequence D
description binding site for residue MG B 502
source : AD1
18) chain B
residue 226
type
sequence D
description binding site for residue MG B 502
source : AD1
19) chain B
residue 216
type
sequence E
description binding site for residue MG B 504
source : AD2
20) chain B
residue 259
type
sequence D
description binding site for residue MG B 504
source : AD2
21) chain B
residue 418
type
sequence D
description binding site for residue MG B 504
source : AD2
22) chain B
residue 91
type
sequence D
description binding site for residue MG B 505
source : AD3
23) chain B
residue 166
type
sequence E
description binding site for residue MG B 505
source : AD3
24) chain B
residue 247
type
sequence D
description binding site for residue MG B 505
source : AD3
25) chain B
residue 95
type
sequence D
description binding site for residue MG B 506
source : AD4
26) chain B
residue 136
type
sequence G
description binding site for residue MG B 506
source : AD4
27) chain B
residue 428
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:19798051
source Swiss-Prot : SWS_FT_FI10
28) chain B
residue 338-351
type TOPO_DOM
sequence IIRALATRDLDLRD
description Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295
source Swiss-Prot : SWS_FT_FI1
29) chain B
residue 410-420
type TOPO_DOM
sequence FLLRRLGVDPA
description Cytoplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295
source Swiss-Prot : SWS_FT_FI1
30) chain B
residue 284-306
type TRANSMEM
sequence ARVRWLVILILTGMVTSSILQGF
description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB
source Swiss-Prot : SWS_FT_FI2
31) chain B
residue 316-337
type TRANSMEM
sequence LAFYVPVLLGTGGNTGNQSATL
description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB
source Swiss-Prot : SWS_FT_FI2
32) chain B
residue 352-381
type TRANSMEM
sequence WRRVFLKEMGVGLLLGLTLSFLLVGKVYWD
description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB
source Swiss-Prot : SWS_FT_FI2
33) chain B
residue 386-409
type TRANSMEM
sequence LLPVVGVSLVLIVFFANLVGAMLP
description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB
source Swiss-Prot : SWS_FT_FI2
34) chain B
residue 421-443
type TRANSMEM
sequence LVSNPLVATLSDVTGLLIYLSVA
description Helical => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9L, ECO:0007744|PDB:4U9N, ECO:0007744|PDB:4WIB
source Swiss-Prot : SWS_FT_FI2
35) chain B
residue 307-315
type TOPO_DOM
sequence ESVLEAVTA
description Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295
source Swiss-Prot : SWS_FT_FI3
36) chain B
residue 382-385
type TOPO_DOM
sequence GHPL
description Periplasmic => ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:25367295
source Swiss-Prot : SWS_FT_FI3
37) chain B
residue 59
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
source Swiss-Prot : SWS_FT_FI4
38) chain B
residue 216
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
source Swiss-Prot : SWS_FT_FI4
39) chain B
residue 255
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
source Swiss-Prot : SWS_FT_FI4
40) chain B
residue 258
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
source Swiss-Prot : SWS_FT_FI4
41) chain B
residue 432
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715
source Swiss-Prot : SWS_FT_FI4
42) chain B
residue 91
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI5
43) chain B
residue 95
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI5
44) chain B
residue 136
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI5
45) chain B
residue 247
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI5
46) chain B
residue 170
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI6
47) chain B
residue 185
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI6
48) chain B
residue 187
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI6
49) chain B
residue 188
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI6
50) chain B
residue 207
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:28747715, ECO:0007744|PDB:5X9G, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI6
51) chain B
residue 223
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI7
52) chain B
residue 226
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI7
53) chain B
residue 250
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9, ECO:0007744|PDB:5X9H
source Swiss-Prot : SWS_FT_FI7
54) chain B
residue 259
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9
source Swiss-Prot : SWS_FT_FI8
55) chain B
residue 418
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:28747715, ECO:0007744|PDB:2ZY9
source Swiss-Prot : SWS_FT_FI8
56) chain B
residue 383
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
source Swiss-Prot : SWS_FT_FI9
57) chain B
residue 275
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
source Swiss-Prot : SWS_FT_FI9
58) chain B
residue 304
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
source Swiss-Prot : SWS_FT_FI9
59) chain B
residue 307
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
source Swiss-Prot : SWS_FT_FI9
60) chain B
residue 311
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:25367295, ECO:0007744|PDB:4U9N
source Swiss-Prot : SWS_FT_FI9

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