eF-site ID 2psn-B
PDB Code 2psn
Chain B

click to enlarge
Title Crystal structure of enolase1
Classification LYASE
Compound Alpha-enolase
Source Homo sapiens (Human) (ENOA_HUMAN)
Sequence B:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST
GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK
LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA
GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN
KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG
KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV
IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK
SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT
VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ
ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLLRIEEELGSKAKFAGRNFRNPLA
Description


Functional site

1) chain B
residue 165
type
sequence Q
description BINDING SITE FOR RESIDUE MG B 703
source : AC3

2) chain B
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE MG B 703
source : AC3

3) chain B
residue 292
type
sequence E
description BINDING SITE FOR RESIDUE MG B 703
source : AC3

4) chain B
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE MG B 703
source : AC3

5) chain B
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE MG B 703
source : AC3

6) chain B
residue 39
type
sequence S
description BINDING SITE FOR RESIDUE MG B 704
source : AC4

7) chain B
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE MG B 704
source : AC4

8) chain B
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE MG B 704
source : AC4

9) chain B
residue 37
type
sequence G
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

10) chain B
residue 38
type
sequence A
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

11) chain B
residue 39
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

12) chain B
residue 157
type
sequence H
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

13) chain B
residue 165
type
sequence Q
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

14) chain B
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

15) chain B
residue 371
type
sequence R
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

16) chain B
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE PO4 B 710
source : BC1

17) chain B
residue 39
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:18560153
source Swiss-Prot : SWS_FT_FI3

18) chain B
residue 244
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18560153
source Swiss-Prot : SWS_FT_FI3

19) chain B
residue 209
type ACT_SITE
sequence E
description Proton donor => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI1

20) chain B
residue 342
type ACT_SITE
sequence K
description Proton acceptor => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 91
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

22) chain B
residue 334
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

23) chain B
residue 342
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

24) chain B
residue 405
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

25) chain B
residue 201
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI11

26) chain B
residue 253
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI13

27) chain B
residue 262
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI14

28) chain B
residue 271
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI15

29) chain B
residue 232
type MOD_RES
sequence K
description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
source Swiss-Prot : SWS_FT_FI12

30) chain B
residue 280
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI16

31) chain B
residue 290
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI17

32) chain B
residue 201
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI18

33) chain B
residue 317
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

34) chain B
residue 369
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

35) chain B
residue 393
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

36) chain B
residue 157
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

37) chain B
residue 166
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

38) chain B
residue 292
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

39) chain B
residue 1
type MOD_RES
sequence S
description N-acetylserine => ECO:0000269|Ref.14, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI5

40) chain B
residue 63
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

41) chain B
residue 70
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

42) chain B
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

43) chain B
residue 192
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

44) chain B
residue 198
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

45) chain B
residue 255
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

46) chain B
residue 284
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

47) chain B
residue 4
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

48) chain B
residue 26
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI7

49) chain B
residue 43
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8

50) chain B
residue 286
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8

51) chain B
residue 59
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI9

52) chain B
residue 88
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI9

53) chain B
residue 227
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI9

54) chain B
residue 419
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI9


Display surface

Download
Links