eF-site ID 2iei-B
PDB Code 2iei
Chain 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 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 B
residue 90
type
sequence Y
description BINDING SITE FOR RESIDUE PLR B 902
source : AC2

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

34) 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

35) 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

36) 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

37) 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

38) 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

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

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

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

42) 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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