eF-site ID 3e3n-B
PDB Code 3e3n
Chain B

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Title The Glycogen phosphorylase b R state- AMP complex
Classification TRANSFERASE
Compound Glycogen phosphorylase, muscle form
Source ORGANISM_COMMON: European rabbit,Japanese white rabbit,domestic rabbit,rabbits; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus;
Sequence B:  QEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVA
TPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLS
LEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIE
EDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIF
NQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRV
EHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSA
KAPNGYIQAVLDRNLAENISRVLYPGKELRLKQEYFVVAA
TLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHP
SLAIPELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPE
ALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDV
DRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEI
LKKTIFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEI
IAERIGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENK
LKFAAYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLH
VITLYNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKL
ITAIGDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADL
SEQISTAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEE
AGEENFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQII
EQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVK
CQERVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAR
EIWGVEPSRQRLPAP
Description


Functional site

1) chain B
residue 42
type
sequence D
description BINDING SITE FOR RESIDUE AMP A 843
source : AC1

2) chain B
residue 44
type
sequence N
description BINDING SITE FOR RESIDUE AMP A 843
source : AC1

3) chain B
residue 45
type
sequence V
description BINDING SITE FOR RESIDUE AMP A 843
source : AC1

4) chain B
residue 43
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 844
source : AC2

5) chain B
residue 67
type
sequence W
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

6) chain B
residue 71
type
sequence Q
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

7) chain B
residue 75
type
sequence Y
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

8) chain B
residue 309
type
sequence R
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

9) chain B
residue 310
type
sequence R
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

10) chain B
residue 315
type
sequence K
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

11) chain B
residue 316
type
sequence F
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

12) chain B
residue 317
type
sequence G
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

13) chain B
residue 318
type
sequence C
description BINDING SITE FOR RESIDUE AMP B 843
source : AC4

14) chain B
residue 14
type
sequence S
description BINDING SITE FOR RESIDUE SO4 B 844
source : AC5

15) chain B
residue 16
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 844
source : AC5

16) chain B
residue 69
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 844
source : AC5

17) chain B
residue 134
type
sequence G
description BINDING SITE FOR RESIDUE SO4 B 845
source : AC6

18) chain B
residue 135
type
sequence G
description BINDING SITE FOR RESIDUE SO4 B 845
source : AC6

19) chain B
residue 569
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 845
source : AC6

20) chain B
residue 574
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 845
source : AC6

21) chain B
residue 377
type catalytic
sequence H
description 205
source MCSA : MCSA2

22) chain B
residue 568
type catalytic
sequence K
description 205
source MCSA : MCSA2

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

24) chain B
residue 574
type catalytic
sequence K
description 205
source MCSA : MCSA2

25) chain B
residue 676
type catalytic
sequence T
description 205
source MCSA : MCSA2

26) chain B
residue 680
type catalytic
sequence X
description 205
source MCSA : MCSA2

27) chain B
residue 14
type MOD_RES
sequence S
description Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI6

28) chain B
residue 42
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI1

29) chain B
residue 309
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P11217
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 75
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:3616621
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 108
type SITE
sequence C
description Involved in the association of subunits => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI3

32) chain B
residue 142
type SITE
sequence C
description Involved in the association of subunits => ECO:0000303|PubMed:728424
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 513
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

34) chain B
residue 746
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI10

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

36) chain B
residue 680
type MOD_RES
sequence X
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

37) chain B
residue 155
type SITE
sequence Y
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 203
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

39) chain B
residue 226
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

40) chain B
residue 429
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
source Swiss-Prot : SWS_FT_FI8

41) chain B
residue 472
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
source Swiss-Prot : SWS_FT_FI9


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