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

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Title Crystal structure of pig phosphoglucose isomerase
Classification ISOMERASE
Compound GLUCOSE-6-PHOSPHATE ISOMERASE
Source ORGANISM_COMMON: PIG; ORGANISM_SCIENTIFIC: SUS SCROFA;
Sequence A:  AALTQNPQFKKLQTWYHEHRSDLNLRRLFEGDKDRFNHFS
LNLNTNHGRILLDYSKNLVTEAVMQMLVDLAKSRGVEAAR
ERMFNGEKINFTEDRAVLHVALRNRSNTPILVDGKDVMPE
VNRVLEKMKSFCKRVRSGEWKGYSGKSITDVINIGIGGSD
LGPLMVTEALKPYSAEGPRVWFVSNIDGTHIAKTLATLNP
ESSLFIIASKTFTTQETITNAETAKEWFLQSAKDPSAVAK
HFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIG
LSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLA
LLGIWYINFFGCETHAMLPYDQYLHRFAAYFQQGDMESNG
KYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKM
IPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMKGKS
TEEARKELQAAGKSPEDFEKLLPHKVFEGNRPTNSIVFTK
LTPFILGALIAMYEHKIFVQGVIWDINSFDQWGVELGKQL
AKKIEPELDGSSPVTSHDSSTNGLINFIKQEREA
Description (1)  GLUCOSE-6-PHOSPHATE ISOMERASE (E.C.5.3.1.9)


Functional site

1) chain A
residue 159
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 1555
source : AC1

2) chain A
residue 209
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 1555
source : AC1

3) chain A
residue 210
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 1555
source : AC1

4) chain A
residue 211
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 1555
source : AC1

5) chain A
residue 214
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 1555
source : AC1

6) chain A
residue 454
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI11

7) chain A
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI4

8) chain A
residue 12
type MOD_RES
sequence L
description N6-acetyllysine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI5

9) chain A
residue 142
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI5

10) chain A
residue 34
type MOD_RES
sequence D
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI6

11) chain A
residue 107
type MOD_RES
sequence N
description Phosphoserine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI7

12) chain A
residue 455
type MOD_RES
sequence P
description Phosphoserine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI7

13) chain A
residue 109
type MOD_RES
sequence P
description Phosphothreonine => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI8

14) chain A
residue 185
type MOD_RES
sequence N
description Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P06744
source Swiss-Prot : SWS_FT_FI9

15) chain A
residue 501-518
type prosite
sequence GVIWDINSFDQWGVELGK
description P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GvIWdinsFDQwGVElgK
source prosite : PS00174

16) chain A
residue 267-280
type prosite
sequence DWVGGRYSLWSAIG
description P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG
source prosite : PS00765

17) chain A
residue 159
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI3

18) chain A
residue 210
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI3

19) chain A
residue 354
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 358
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 389
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 519
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI3

23) chain A
residue 358
type ACT_SITE
sequence S
description Proton donor => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 250
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0
source Swiss-Prot : SWS_FT_FI10

25) chain A
residue 389
type ACT_SITE
sequence A
description ACT_SITE => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 519
type ACT_SITE
sequence Q
description ACT_SITE => ECO:0000250|UniProtKB:P06745
source Swiss-Prot : SWS_FT_FI2


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