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

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Title Glycogen Phosphorylase b in complex with N-4-phenylbenzoyl-N'-beta-D-glucopyranosyl urea
Classification TRANSFERASE
Compound Glycogen phosphorylase, muscle form
Source ORGANISM_COMMON: Rabbit; ORGANISM_SCIENTIFIC: Oryctolagus cuniculus;
Sequence A:  QISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDY
YFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYM
GRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGL
GNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIC
GGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQ
GAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPND
FNLGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEY
FVVAATLQDIIRRFKSSTNFDAFPDKVAIQLNDTHPSLAI
PELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVLPEALER
WPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLR
RMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKT
IFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAER
IGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFA
AYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITL
YNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAI
GDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQI
STAGTEASGTGNMXFMLNGALTIGTMDGANVEMAEEAGEE
NFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLS
SGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQER
VSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWG
VEPSRQRLPA
Description


Functional site

1) chain A
residue 88
type
sequence E
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

2) chain A
residue 133
type
sequence N
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

3) chain A
residue 135
type
sequence G
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

4) chain A
residue 136
type
sequence L
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

5) chain A
residue 282
type
sequence N
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

6) chain A
residue 292
type
sequence R
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

7) chain A
residue 341
type
sequence H
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

8) chain A
residue 377
type
sequence H
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

9) chain A
residue 385
type
sequence E
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

10) chain A
residue 484
type
sequence N
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

11) chain A
residue 573
type
sequence Y
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

12) chain A
residue 672
type
sequence E
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

13) chain A
residue 673
type
sequence A
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

14) chain A
residue 674
type
sequence S
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

15) chain A
residue 675
type
sequence G
description BINDING SITE FOR RESIDUE F59 A 998
source : AC1

16) chain A
residue 377
type catalytic
sequence H
description 205
source MCSA : MCSA1

17) chain A
residue 568
type catalytic
sequence K
description 205
source MCSA : MCSA1

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

19) chain A
residue 574
type catalytic
sequence K
description 205
source MCSA : MCSA1

20) chain A
residue 676
type catalytic
sequence T
description 205
source MCSA : MCSA1

21) chain A
residue 680
type catalytic
sequence X
description 205
source MCSA : MCSA1

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

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

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

25) chain A
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

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

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

28) chain A
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

29) chain A
residue 203
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P09812
source Swiss-Prot : SWS_FT_FI7

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

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

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

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

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

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

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

37) chain A
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


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