eF-site ID 6o4x-A
PDB Code 6o4x
Chain A

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Title Binary complex of native hAChE with 9-aminoacridine
Classification HYDROLASE
Compound Acetylcholinesterase
Source (ACES_HUMAN)
Sequence A:  EDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMG
PRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGT
EMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGF
YSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPG
SREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGES
AGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGE
ARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVN
HEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHG
LQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGV
RVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVG
DHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWM
GVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANF
ARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRG
LRAQACAFWNRFLPKLLSAT
Description


Functional site

1) chain A
residue 124
type
sequence Y
description binding site for residue GOL A 601
source : AC1

2) chain A
residue 294
type
sequence V
description binding site for residue GOL A 601
source : AC1

3) chain A
residue 295
type
sequence F
description binding site for residue GOL A 601
source : AC1

4) chain A
residue 297
type
sequence F
description binding site for residue GOL A 601
source : AC1

5) chain A
residue 337
type
sequence Y
description binding site for residue GOL A 601
source : AC1

6) chain A
residue 338
type
sequence F
description binding site for residue GOL A 601
source : AC1

7) chain A
residue 341
type
sequence Y
description binding site for residue GOL A 601
source : AC1

8) chain A
residue 81
type
sequence E
description binding site for residue GOL A 602
source : AC2

9) chain A
residue 85
type
sequence M
description binding site for residue GOL A 602
source : AC2

10) chain A
residue 436
type
sequence T
description binding site for residue GOL A 602
source : AC2

11) chain A
residue 437
type
sequence L
description binding site for residue GOL A 602
source : AC2

12) chain A
residue 438
type
sequence S
description binding site for residue GOL A 602
source : AC2

13) chain A
residue 452
type
sequence E
description binding site for residue GOL A 602
source : AC2

14) chain A
residue 465
type
sequence Y
description binding site for residue GOL A 602
source : AC2

15) chain A
residue 332
type
sequence K
description binding site for residue GOL A 603
source : AC3

16) chain A
residue 429
type
sequence V
description binding site for residue GOL A 603
source : AC3

17) chain A
residue 431
type
sequence E
description binding site for residue GOL A 603
source : AC3

18) chain A
residue 510
type
sequence Y
description binding site for residue GOL A 603
source : AC3

19) chain A
residue 521
type
sequence R
description binding site for residue GOL A 603
source : AC3

20) chain A
residue 525
type
sequence R
description binding site for residue GOL A 603
source : AC3

21) chain A
residue 332
type
sequence K
description binding site for residue NO3 A 604
source : AC4

22) chain A
residue 333
type
sequence D
description binding site for residue NO3 A 604
source : AC4

23) chain A
residue 396
type
sequence E
description binding site for residue NO3 A 604
source : AC4

24) chain A
residue 442
type
sequence W
description binding site for residue NO3 A 604
source : AC4

25) chain A
residue 444
type
sequence G
description binding site for residue NO3 A 604
source : AC4

26) chain A
residue 86
type
sequence W
description binding site for residue AA A 605
source : AC5

27) chain A
residue 120
type
sequence G
description binding site for residue AA A 605
source : AC5

28) chain A
residue 121
type
sequence G
description binding site for residue AA A 605
source : AC5

29) chain A
residue 202
type
sequence E
description binding site for residue AA A 605
source : AC5

30) chain A
residue 337
type
sequence Y
description binding site for residue AA A 605
source : AC5

31) chain A
residue 439
type
sequence W
description binding site for residue AA A 605
source : AC5

32) chain A
residue 447
type
sequence H
description binding site for residue AA A 605
source : AC5

33) chain A
residue 190-205
type prosite
sequence FGGDPTSVTLFGESAG
description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG
source prosite : PS00122

34) chain A
residue 203
type ACT_SITE
sequence S
description Acyl-ester intermediate
source Swiss-Prot : SWS_FT_FI1

35) chain A
residue 334
type ACT_SITE
sequence E
description Charge relay system
source Swiss-Prot : SWS_FT_FI2

36) chain A
residue 447
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 86
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:4EY5
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 133
type BINDING
sequence Y
description BINDING => ECO:0007744|PDB:4EY5
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 337
type BINDING
sequence Y
description BINDING => ECO:0007744|PDB:4EY5
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 122
type BINDING
sequence G
description BINDING => ECO:0007744|PDB:4BDT
source Swiss-Prot : SWS_FT_FI4

41) chain A
residue 439
type BINDING
sequence W
description BINDING => ECO:0007744|PDB:4BDT
source Swiss-Prot : SWS_FT_FI4

42) chain A
residue 447
type BINDING
sequence H
description BINDING => ECO:0007744|PDB:4BDT
source Swiss-Prot : SWS_FT_FI4

43) chain A
residue 203
type BINDING
sequence S
description BINDING => ECO:0007744|PDB:4BDT
source Swiss-Prot : SWS_FT_FI4

44) chain A
residue 202
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:4EY6
source Swiss-Prot : SWS_FT_FI5

45) chain A
residue 265
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7
source Swiss-Prot : SWS_FT_FI6

46) chain A
residue 350
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11053835, ECO:0000269|PubMed:20408548, ECO:0000269|PubMed:23035744, ECO:0000269|PubMed:23679855, ECO:0007744|PDB:1B41, ECO:0007744|PDB:1F8U, ECO:0007744|PDB:2X8B, ECO:0007744|PDB:4BDT, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7, ECO:0007744|PDB:4EY8
source Swiss-Prot : SWS_FT_FI7

47) chain A
residue 464
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY8
source Swiss-Prot : SWS_FT_FI8

48) chain A
residue 94-104
type prosite
sequence EDCLYLNVWTP
description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP
source prosite : PS00941


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