eF-site ID 1qxs-C
PDB Code 1qxs
Chain C

click to enlarge
Title CRYSTAL STRUCTURE OF Trypanosoma cruzi GLYCERALDEHYDE-3- PHOSPHATE DEHYDROGENASE COMPLEXED WITH AN ANALOGUE OF 1,3- BisPHOSPHO-D-GLYCERIC ACID
Classification OXIDOREDUCTASE
Compound Glyceraldehyde 3-phosphate dehydrogenase, glycosomal
Source null (G3PG_TRYCR)
Sequence C:  MPIKVGINGFGRIGRMVFQALCEDGLLGTEIDVVAVVDMN
TDAEYFAYQMRYDTVHGKFKYEVTTTKSSPSVAKDDTLVV
NGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTAKAAA
EGHLRGGARKVVISAPASGGAKTLVMGVNHHEYNPSEHHV
VSNASCTTNCLAPIVHVLVKEGFGVQTGLMTTIHSYTATQ
KTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTQ
GKLTGMSFRVPTPDVSVVDLTFTAARDTSIQEIDAALKRA
SKTYMKGILGYTDEELVSADFINDNRSSIYDSKATLQNNL
PKERRFFKIVSWYDNEWGYSHRVVDLVRHMASKDRSARL
Description


Functional site

1) chain C
residue 8
type
sequence N
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

2) chain C
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

3) chain C
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

4) chain C
residue 12
type
sequence R
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

5) chain C
residue 13
type
sequence I
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

6) chain C
residue 38
type
sequence D
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

7) chain C
residue 39
type
sequence M
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

8) chain C
residue 91
type
sequence Q
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

9) chain C
residue 110
type
sequence S
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

10) chain C
residue 111
type
sequence T
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

11) chain C
residue 112
type
sequence G
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

12) chain C
residue 113
type
sequence L
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

13) chain C
residue 134
type
sequence S
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

14) chain C
residue 135
type
sequence A
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

15) chain C
residue 166
type
sequence C
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

16) chain C
residue 198
type
sequence A
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

17) chain C
residue 335
type
sequence N
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

18) chain C
residue 339
type
sequence Y
description BINDING SITE FOR RESIDUE NAD C 860
source : AC1

19) chain C
residue 206
type
sequence V
description BINDING SITE FOR RESIDUE NAD B 863
source : AC4

20) chain C
residue 166
type ACT_SITE
sequence C
description Nucleophile
source Swiss-Prot : SWS_FT_FI1

21) chain C
residue 249
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

22) chain C
residue 165
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI3

23) chain C
residue 197
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

24) chain C
residue 226
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

25) chain C
residue 194
type SITE
sequence H
description Activates thiol group during catalysis
source Swiss-Prot : SWS_FT_FI4

26) chain C
residue 164-171
type prosite
sequence ASCTTNCL
description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
source prosite : PS00071

27) chain C
residue 38
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286
source Swiss-Prot : SWS_FT_FI2

28) chain C
residue 335
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286
source Swiss-Prot : SWS_FT_FI2

29) chain C
residue 91
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286
source Swiss-Prot : SWS_FT_FI2

30) chain C
residue 134
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286
source Swiss-Prot : SWS_FT_FI2

31) chain C
residue 12
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286
source Swiss-Prot : SWS_FT_FI2


Display surface

Download
Links