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

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


Functional site

1) chain A
residue 165
type
sequence Q
description BINDING SITE FOR RESIDUE MG A 701
source : AC1

2) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE MG A 701
source : AC1

3) chain A
residue 292
type
sequence E
description BINDING SITE FOR RESIDUE MG A 701
source : AC1

4) chain A
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE MG A 701
source : AC1

5) chain A
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE MG A 701
source : AC1

6) chain A
residue 39
type
sequence S
description BINDING SITE FOR RESIDUE MG A 702
source : AC2

7) chain A
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE MG A 702
source : AC2

8) chain A
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE MG A 702
source : AC2

9) chain A
residue 37
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

10) chain A
residue 38
type
sequence A
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

11) chain A
residue 39
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

12) chain A
residue 157
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

13) chain A
residue 165
type
sequence Q
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

14) chain A
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

15) chain A
residue 371
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

16) chain A
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 709
source : AC9

17) chain A
residue 339-352
type prosite
sequence LLLKVNQIGSVTES
description ENOLASE Enolase signature. LLLKvNQIGSVTES
source prosite : PS00164

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

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

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

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

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

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

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

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

26) chain A
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

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

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

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

30) chain A
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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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