eF-site ID 6a94-A
PDB Code 6a94
Chain A

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Title Crystal structure of 5-HT2AR in complex with zotepine
Classification MEMBRANE PROTEIN
Compound 5-hydroxytryptamine receptor 2A,Soluble cytochrome b562
Source (5HT2A_HUMAN)
Sequence A:  THLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNA
TNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLC
AVWIYLDVLFSTAKIWHLCAISLDRYVAIQNPIHHSRFNS
RTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCL
LADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEAADL
EDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAGSG
SGDILVGQIDDALKLANEGKVKEAQAAAEQLKTTINAYIQ
KYGQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVIC
KESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRS
AFSRYIQCQY
Description


Functional site

1) chain A
residue 155
type
sequence D
description binding site for residue ZOT A 3001
source : AC1

2) chain A
residue 159
type
sequence S
description binding site for residue ZOT A 3001
source : AC1

3) chain A
residue 229
type
sequence L
description binding site for residue ZOT A 3001
source : AC1

4) chain A
residue 235
type
sequence V
description binding site for residue ZOT A 3001
source : AC1

5) chain A
residue 238
type
sequence G
description binding site for residue ZOT A 3001
source : AC1

6) chain A
residue 242
type
sequence S
description binding site for residue ZOT A 3001
source : AC1

7) chain A
residue 336
type
sequence W
description binding site for residue ZOT A 3001
source : AC1

8) chain A
residue 339
type
sequence F
description binding site for residue ZOT A 3001
source : AC1

9) chain A
residue 340
type
sequence F
description binding site for residue ZOT A 3001
source : AC1

10) chain A
residue 343
type
sequence N
description binding site for residue ZOT A 3001
source : AC1

11) chain A
residue 111
type
sequence Y
description binding site for residue CLR A 3002
source : AC2

12) chain A
residue 114
type
sequence M
description binding site for residue CLR A 3002
source : AC2

13) chain A
residue 118
type
sequence I
description binding site for residue CLR A 3002
source : AC2

14) chain A
residue 122
type
sequence L
description binding site for residue CLR A 3002
source : AC2

15) chain A
residue 153
type
sequence Y
description binding site for residue CLR A 3002
source : AC2

16) chain A
residue 193
type
sequence F
description binding site for residue CLR A 3002
source : AC2

17) chain A
residue 196
type
sequence I
description binding site for residue CLR A 3002
source : AC2

18) chain A
residue 200
type
sequence W
description binding site for residue CLR A 3002
source : AC2

19) chain A
residue 204
type
sequence V
description binding site for residue CLR A 3002
source : AC2

20) chain A
residue 261
type
sequence L
description binding site for residue 1PE A 3003
source : AC3

21) chain A
residue 262
type
sequence Q
description binding site for residue 1PE A 3003
source : AC3

22) chain A
residue 265
type
sequence A
description binding site for residue 1PE A 3003
source : AC3

23) chain A
residue 315
type
sequence I
description binding site for residue 1PE A 3003
source : AC3

24) chain A
residue 316
type
sequence S
description binding site for residue 1PE A 3003
source : AC3

25) chain A
residue 319
type
sequence Q
description binding site for residue 1PE A 3003
source : AC3

26) chain A
residue 1004
type
sequence E
description binding site for residue 1PE A 3003
source : AC3

27) chain A
residue 1080
type
sequence N
description binding site for residue 1PE A 3003
source : AC3

28) chain A
residue 182
type
sequence H
description binding site for residue ZN A 3004
source : AC4

29) chain A
residue 183
type
sequence H
description binding site for residue ZN A 3004
source : AC4

30) chain A
residue 264
type
sequence E
description binding site for residue ZN A 3004
source : AC4

31) chain A
residue 318
type
sequence E
description binding site for residue ZN A 3004
source : AC4

32) chain A
residue 253
type
sequence T
description binding site for residue A6L B 3004
source : AC8

33) chain A
residue 256
type
sequence L
description binding site for residue A6L B 3004
source : AC8

34) chain A
residue 1007
type BINDING
sequence W
description axial binding residue
source Swiss-Prot : SWS_FT_FI12

35) chain A
residue 1102
type BINDING
sequence I
description axial binding residue
source Swiss-Prot : SWS_FT_FI12

36) chain A
residue 229
type SITE
sequence L
description Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538
source Swiss-Prot : SWS_FT_FI11

37) chain A
residue 76-99
type TRANSMEM
sequence WSALLTAVVIILTIAGNILVIMAV
description Helical; Name=1 => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

38) chain A
residue 100-110
type TOPO_DOM
sequence SLEKKLQNATN
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 172-191
type TOPO_DOM
sequence DRYVAIQNPIHHSRFNSRTK
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 111-132
type TRANSMEM
sequence YFLMSLAIADMLLGFLVMPVSM
description Helical; Name=2 => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 133-148
type TOPO_DOM
sequence LTILYGYRWPLPSKLC
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

42) chain A
residue 216-233
type TOPO_DOM
sequence QDDSKVFKEGSCLLADDN
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

43) chain A
residue 347-362
type TOPO_DOM
sequence VICKESCNEDVIGALL
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

44) chain A
residue 149-171
type TRANSMEM
sequence AVWIYLDVLFSTAKIWHLCAISL
description Helical; Name=3 => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

45) chain A
residue 192-215
type TRANSMEM
sequence AFLKIIAVWTISVGISMPIPVFGL
description Helical; Name=4 => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

46) chain A
residue 234-254
type TRANSMEM
sequence FVLIGSFVSFFIPLTIMVITY
description Helical; Name=5 => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

47) chain A
residue 325-346
type TRANSMEM
sequence LGIVFFLFVVMWCPFFITNIMA
description Helical; Name=6 => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

48) chain A
residue 363-384
type TRANSMEM
sequence NVFVWIGYLSSAVNPLVYTLFN
description Helical; Name=7 => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

49) chain A
residue 229
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P41595
source Swiss-Prot : SWS_FT_FI10

50) chain A
residue 155
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P41595
source Swiss-Prot : SWS_FT_FI10

51) chain A
residue 160
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P41595
source Swiss-Prot : SWS_FT_FI10


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