eF-site ID 2iei-AB
PDB Code 2iei
Chain A, B

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Title Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone
Classification TRANSFERASE
Compound Glycogen phosphorylase, muscle form
Source ORGANISM_COMMON: rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus;
Sequence A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY
YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM
GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL
GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC
GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSG
AKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPYIQ
AVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATL
QDIIRRFKSFDAFPDKVAIQLNDTHPSLAIPELMRVLVDL
ERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETLL
PRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGAV
KRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEP
HKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDLD
QLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYVHI
NPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNKF
VVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVVG
DRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGTG
NMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVED
VDRLDQRGYNAQEYYDRIPELRQIIEQLSSGFFSPKQPDL
FKDIVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREW
TRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSR
B:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY
YFALAHTVRDHLVGRWIRTQQHYKDPKRIYYLSLEFYMGR
TLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGN
GGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGG
WQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGA
KWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPGYIQ
AVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATL
QDIIRRFKSNFDAFPDKVAIQLNDTHPSLAIPELMRVLVD
LERLDWDKAWEVTVKTCAYTNHTVIPEALERWPVHLLETL
LPRHLQIIYEINQRFLNRVAAAFPGDVDRLRRMSLVEEGA
VKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELE
PHKFQNKTNGITPRRWLVLCNPGLAEIIAERIGEEYISDL
DQLRKLLSYVDDEAFIRDVAKVKQENKLKFAAYLEREYKH
INPNSLFDVQVKRIHEYKRQLLNCLHVITLYNRIKKEPNK
FVVPRTVMIGGKAAPGYHMAKMIIKLITAIGDVVNHDPVV
GDRLRVIFLENYRVSLAEKVIPAADLSEQISTAGTEASGT
GNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVE
DVDRLDNAQEYYDRIPELRQIIEQLSSGFFSPKQPDLFKD
IVNMLMHHDRFKVFADYEEYVKCQERVSALYKNPREWTRM
VIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPA
Description (1)  Glycogen phosphorylase, muscle form (E.C.2.4.1.1)


Functional site

1) chain A
residue 134
type
sequence G
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

2) chain A
residue 135
type
sequence G
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

3) chain A
residue 568
type
sequence K
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

4) chain A
residue 574
type
sequence K
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

5) chain A
residue 648
type
sequence Y
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

6) chain A
residue 649
type
sequence R
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

7) chain A
residue 650
type
sequence V
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

8) chain A
residue 675
type
sequence G
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

9) chain A
residue 676
type
sequence T
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

10) chain A
residue 677
type
sequence G
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

11) chain A
residue 680
type
sequence K
description BINDING SITE FOR RESIDUE PLR A 901
source : AC1

12) chain B
residue 90
type
sequence Y
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

13) chain B
residue 134
type
sequence G
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

14) chain B
residue 135
type
sequence G
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

15) chain B
residue 491
type
sequence W
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

16) chain B
residue 568
type
sequence K
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

17) chain B
residue 648
type
sequence Y
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

18) chain B
residue 649
type
sequence R
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

19) chain B
residue 650
type
sequence V
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

20) chain B
residue 675
type
sequence G
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

21) chain B
residue 676
type
sequence T
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

22) chain B
residue 677
type
sequence G
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

23) chain B
residue 680
type
sequence K
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

24) chain A
residue 38
type
sequence T
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

25) chain A
residue 40
type
sequence V
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

26) chain A
residue 53
type
sequence F
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

27) chain A
residue 57
type
sequence H
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

28) chain A
residue 60
type
sequence R
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

29) chain A
residue 185
type
sequence Y
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

30) chain B
residue 60
type
sequence R
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

31) chain B
residue 67
type
sequence W
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

32) chain B
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

33) chain B
residue 191
type
sequence K
description BINDING SITE FOR RESIDUE FRX B 903
source : AC3

34) chain A
residue 60
type
sequence R
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

35) chain A
residue 188
type
sequence P
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

36) chain A
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

37) chain A
residue 191
type
sequence K
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

38) chain A
residue 192
type
sequence A
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

39) chain B
residue 38
type
sequence T
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

40) chain B
residue 39
type
sequence L
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

41) chain B
residue 40
type
sequence V
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

42) chain B
residue 57
type
sequence H
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

43) chain B
residue 184
type
sequence R
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

44) chain B
residue 185
type
sequence Y
description BINDING SITE FOR RESIDUE FRX A 904
source : AC4

45) chain A
residue 378
type catalytic
sequence T
description 205
source MCSA : MCSA1

46) chain A
residue 569
type catalytic
sequence R
description 205
source MCSA : MCSA1

47) chain A
residue 570
type catalytic
sequence I
description 205
source MCSA : MCSA1

48) chain A
residue 575
type catalytic
sequence R
description 205
source MCSA : MCSA1

49) chain A
residue 677
type catalytic
sequence G
description 205
source MCSA : MCSA1

50) chain A
residue 681
type catalytic
sequence F
description 205
source MCSA : MCSA1

51) chain B
residue 378
type catalytic
sequence T
description 205
source MCSA : MCSA2

52) chain B
residue 569
type catalytic
sequence R
description 205
source MCSA : MCSA2

53) chain B
residue 570
type catalytic
sequence I
description 205
source MCSA : MCSA2

54) chain B
residue 575
type catalytic
sequence R
description 205
source MCSA : MCSA2

55) chain B
residue 677
type catalytic
sequence G
description 205
source MCSA : MCSA2

56) chain B
residue 681
type catalytic
sequence F
description 205
source MCSA : MCSA2

57) chain A
residue 672-684
type prosite
sequence EASGTGNMKFMLN
description PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN
source prosite : PS00102

58) chain A
residue 43
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI1

59) chain A
residue 310
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI1

60) chain B
residue 43
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI1

61) chain B
residue 310
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI1

62) chain A
residue 514
type MOD_RES
sequence D
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

63) chain A
residue 747
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

64) chain A
residue 748
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

65) chain B
residue 514
type MOD_RES
sequence D
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

66) chain B
residue 747
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

67) chain B
residue 748
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

68) chain A
residue 681
type MOD_RES
sequence F
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE
source Swiss-Prot : SWS_FT_FI11

69) chain B
residue 681
type MOD_RES
sequence F
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE
source Swiss-Prot : SWS_FT_FI11

70) chain A
residue 76
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:3616621
source Swiss-Prot : SWS_FT_FI2

71) chain A
residue 109
type SITE
sequence D
description Involved in the association of subunits => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI3

72) chain A
residue 143
type SITE
sequence F
description Involved in the association of subunits => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI3

73) chain B
residue 109
type SITE
sequence D
description Involved in the association of subunits => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI3

74) chain B
residue 143
type SITE
sequence F
description Involved in the association of subunits => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI3

75) chain A
residue 156
type SITE
sequence G
description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI4

76) chain B
residue 156
type SITE
sequence G
description Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI4

77) chain A
residue 15
type MOD_RES
sequence V
description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI6

78) chain B
residue 15
type MOD_RES
sequence V
description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI6

79) chain A
residue 204
type MOD_RES
sequence G
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

80) chain A
residue 227
type MOD_RES
sequence D
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

81) chain B
residue 204
type MOD_RES
sequence G
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

82) chain B
residue 227
type MOD_RES
sequence D
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

83) chain A
residue 430
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
source Swiss-Prot : SWS_FT_FI8

84) chain B
residue 430
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
source Swiss-Prot : SWS_FT_FI8

85) chain A
residue 473
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
source Swiss-Prot : SWS_FT_FI9

86) chain B
residue 473
type MOD_RES
sequence E
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
source Swiss-Prot : SWS_FT_FI9


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