eF-site ID 1p4g-A
PDB Code 1p4g
Chain A

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Title Crystal structure of glycogen phosphorylase b in complex with C-(1-azido-alpha-D-glucopyranosyl)formamide
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
PELMRVLVDLERLDWDKAWEVTVKTCAYTNHTVIPEALER
WPVHLLETLLPRHLQIIYEINQRFLNRVAAAFPGDVDRLR
RMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKT
IFKDFYELEPHKFQNKTNGITPRRWLVLCNPGLAEIIAER
IGEEYISDLDQLRKLLSYVDDEAFIRDVAKVKQENKLKFA
AYLEREYKVHINPNSLFDVQVKRIHEYKRQLLNCLHVITL
YNRIKKEPNKFVVPRTVMIGGKAAPGYHMAKMIIKLITAI
GDVVNHDPVVGDRLRVIFLENYRVSLAEKVIPAADLSEQI
STAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEE
NFFIFGMRVEDVDRLDQRGYNAQEYYDRIPELRQIIEQLS
SGFFSPKQPDLFKDIVNMLMHHDRFKVFADYEEYVKCQER
VSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWG
VEPSRQRLPA
Description


Functional site

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

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

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

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

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

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

7) 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

8) 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

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

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

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

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

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

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

15) 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

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

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

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

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

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

21) 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

22) 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


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