eF-site ID 1te6-AB
PDB Code 1te6
Chain A, B

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Title Crystal Structure of Human Neuron Specific Enolase at 1.8 angstrom
Classification LYASE
Compound Gamma enolase
Source Homo sapiens (Human) (ENOG_HUMAN)
Sequence A:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST
GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG
LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA
GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN
KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG
KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV
IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ
DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT
VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ
ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVLH
B:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST
GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG
LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA
GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN
KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG
KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV
IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ
DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT
VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ
ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL
Description


Functional site

1) chain A
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE MG A 640
source : AC1

2) chain A
residue 292
type
sequence E
description BINDING SITE FOR RESIDUE MG A 640
source : AC1

3) chain A
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE MG A 640
source : AC1

4) chain A
residue 39
type
sequence S
description BINDING SITE FOR RESIDUE MG A 641
source : AC2

5) chain A
residue 37
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

6) chain A
residue 38
type
sequence A
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

7) chain A
residue 39
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

8) chain A
residue 157
type
sequence H
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

9) chain A
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

10) chain A
residue 371
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

11) chain A
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE PO4 A 642
source : AC3

12) chain B
residue 244
type
sequence D
description BINDING SITE FOR RESIDUE MG B 740
source : AC4

13) chain B
residue 292
type
sequence E
description BINDING SITE FOR RESIDUE MG B 740
source : AC4

14) chain B
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE MG B 740
source : AC4

15) chain B
residue 342
type
sequence K
description BINDING SITE FOR RESIDUE CL B 742
source : AC5

16) chain B
residue 371
type
sequence R
description BINDING SITE FOR RESIDUE CL B 742
source : AC5

17) chain B
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE CL B 742
source : AC5

18) chain A
residue 40
type
sequence T
description BINDING SITE FOR RESIDUE TRS A 660
source : AC6

19) chain A
residue 249
type
sequence E
description BINDING SITE FOR RESIDUE TRS A 660
source : AC6

20) chain A
residue 297
type
sequence Q
description BINDING SITE FOR RESIDUE TRS A 660
source : AC6

21) chain A
residue 210
type ACT_SITE
sequence G
description Proton donor => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 210
type ACT_SITE
sequence G
description Proton donor => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 343
type ACT_SITE
sequence V
description Proton acceptor => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI2

24) chain B
residue 343
type ACT_SITE
sequence V
description Proton acceptor => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 158
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

26) chain B
residue 318
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

27) chain B
residue 370
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

28) chain B
residue 394
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

29) chain A
residue 167
type BINDING
sequence F
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

30) chain A
residue 293
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

31) chain A
residue 318
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

32) chain A
residue 370
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

33) chain A
residue 394
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

34) chain B
residue 158
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

35) chain B
residue 167
type BINDING
sequence F
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

36) chain B
residue 293
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P00924
source Swiss-Prot : SWS_FT_FI4

37) chain A
residue 245
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI5

38) chain B
residue 245
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI5

39) chain A
residue 263
type MOD_RES
sequence P
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI14

40) chain B
residue 263
type MOD_RES
sequence P
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI14

41) chain A
residue 287
type MOD_RES
sequence P
description Phosphotyrosine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI15

42) chain B
residue 287
type MOD_RES
sequence P
description Phosphotyrosine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI15

43) chain A
residue 291
type MOD_RES
sequence I
description Phosphoserine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI16

44) chain B
residue 291
type MOD_RES
sequence I
description Phosphoserine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI16

45) chain A
residue 335
type MOD_RES
sequence A
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI17

46) chain A
residue 343
type MOD_RES
sequence V
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI17

47) chain A
residue 406
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI17

48) chain B
residue 335
type MOD_RES
sequence A
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI17

49) chain B
residue 343
type MOD_RES
sequence V
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI17

50) chain B
residue 406
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI17

51) chain A
residue 202
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI18

52) chain B
residue 202
type CROSSLNK
sequence D
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI18

53) chain A
residue 2
type MOD_RES
sequence I
description N-acetylserine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI6

54) chain B
residue 2
type MOD_RES
sequence I
description N-acetylserine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI6

55) chain A
residue 5
type MOD_RES
sequence I
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

56) chain A
residue 64
type MOD_RES
sequence A
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

57) chain A
residue 193
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

58) chain A
residue 256
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

59) chain B
residue 5
type MOD_RES
sequence I
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

60) chain B
residue 64
type MOD_RES
sequence A
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

61) chain B
residue 193
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

62) chain B
residue 256
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI7

63) chain A
residue 26
type MOD_RES
sequence A
description Phosphothreonine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI8

64) chain B
residue 26
type MOD_RES
sequence A
description Phosphothreonine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI8

65) chain A
residue 44
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI9

66) chain B
residue 44
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI9

67) chain A
residue 339-352
type prosite
sequence LLLKVNQIGSVTEA
description ENOLASE Enolase signature. LLLKvNQIGSVTEA
source prosite : PS00164

68) chain A
residue 40
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI3

69) chain B
residue 40
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI3

70) chain A
residue 60
type MOD_RES
sequence G
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

71) chain A
residue 89
type MOD_RES
sequence L
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

72) chain A
residue 228
type MOD_RES
sequence E
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

73) chain B
residue 60
type MOD_RES
sequence G
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

74) chain B
residue 89
type MOD_RES
sequence L
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

75) chain B
residue 228
type MOD_RES
sequence E
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI10

76) chain A
residue 197
type MOD_RES
sequence D
description N6-acetyllysine => ECO:0000250|UniProtKB:P17183
source Swiss-Prot : SWS_FT_FI11

77) chain A
residue 199
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000250|UniProtKB:P17183
source Swiss-Prot : SWS_FT_FI11

78) chain B
residue 197
type MOD_RES
sequence D
description N6-acetyllysine => ECO:0000250|UniProtKB:P17183
source Swiss-Prot : SWS_FT_FI11

79) chain B
residue 199
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0000250|UniProtKB:P17183
source Swiss-Prot : SWS_FT_FI11

80) chain A
residue 202
type MOD_RES
sequence D
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI12

81) chain B
residue 202
type MOD_RES
sequence D
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182
source Swiss-Prot : SWS_FT_FI12

82) chain A
residue 233
type MOD_RES
sequence A
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI13

83) chain B
residue 233
type MOD_RES
sequence A
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733
source Swiss-Prot : SWS_FT_FI13


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