eF-site ID 5jqq-A
PDB Code 5jqq
Chain A

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Title Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis - apo form
Classification TRANSFERASE
Compound Glucosyl-3-phosphoglycerate synthase
Source Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (GPGS_MYCTU)
Sequence A:  TTWHRPGWTIGELEAAKAGRTISVVLPALNEEATIESVID
SISPLVDGLVDELIVLDSGSTDDTEIRAIASGARVVSREQ
ALPEVPVRPGKGEALWRSLAATSGDIVVFIDSDLINPHPL
FVPWLVGPLLTGEGIQLVKSFYRGGRVTELVARPLLAALR
PELGCVLQPLSGEYAASRELLTSLPFAPGYGVEIGLLIDT
FDRLGLDAIAQVNLGVRAHRNRPLDELGAMSRQVIATLLS
RCGIPDSGVGLTQFLDYTRHTWPVSLVDRPPMKVMR
Description


Functional site

1) chain A
residue 184
type
sequence G
description binding site for residue GOL A 401
source : AC1

2) chain A
residue 185
type
sequence R
description binding site for residue GOL A 401
source : AC1

3) chain A
residue 187
type
sequence T
description binding site for residue GOL A 401
source : AC1

4) chain A
residue 258
type
sequence H
description binding site for residue GOL A 401
source : AC1

5) chain A
residue 261
type
sequence R
description binding site for residue GOL A 401
source : AC1

6) chain A
residue 50
type
sequence P
description binding site for residue GOL A 402
source : AC2

7) chain A
residue 51
type
sequence A
description binding site for residue GOL A 402
source : AC2

8) chain A
residue 52
type
sequence L
description binding site for residue GOL A 402
source : AC2

9) chain A
residue 54
type
sequence E
description binding site for residue GOL A 402
source : AC2

10) chain A
residue 134
type
sequence D
description binding site for residue GOL A 402
source : AC2

11) chain A
residue 135
type
sequence S
description binding site for residue GOL A 402
source : AC2

12) chain A
residue 260
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U
source Swiss-Prot : SWS_FT_FI4

13) chain A
residue 184
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:26136334, ECO:0000269|PubMed:28625787, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y9X, ECO:0007744|PDB:5JQX
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 256
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:28625787, ECO:0007744|PDB:5JT0
source Swiss-Prot : SWS_FT_FI3

15) chain A
residue 50
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 81
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 114
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 134
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 136
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 229
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 258
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X
source Swiss-Prot : SWS_FT_FI1


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