eF-site ID 6i2p-B
PDB Code 6i2p
Chain B

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Title Crystal structure of the Mycobacterium tuberculosis PknB kinase domain (L33E mutant) in complex with its substrate GarA
Classification SIGNALING PROTEIN
Compound Serine/threonine-protein kinase PknB
Source (6I2P)
Sequence B:  TTPSHLSDRYELGEILGFGGMSEVHLARDLREHRDVAVKV
LRADLARDPSFYLRFRREAQNAAALNHPAIVAVYDTGEAE
TPAGPLPYIVMEYVDGVTLRDIVHTEGPMTPKRAIEVIAD
ACQALNFSHQNGIIHRDVKPANIMISATNAVKVMDFGIAN
SVXQXAATAQYLSPEQARGDSVDARSDVYSLGCVLYEVLT
GEPPFTGDSPVSVAYQHVREDPIPPSARHEGLSADLDAVV
LKALAKNPENRYQTAAEMRADLVRVH
Description


Functional site

1) chain B
residue 18
type
sequence G
description binding site for residue ACP B 301
source : AC4

2) chain B
residue 19
type
sequence F
description binding site for residue ACP B 301
source : AC4

3) chain B
residue 20
type
sequence G
description binding site for residue ACP B 301
source : AC4

4) chain B
residue 21
type
sequence G
description binding site for residue ACP B 301
source : AC4

5) chain B
residue 23
type
sequence S
description binding site for residue ACP B 301
source : AC4

6) chain B
residue 25
type
sequence V
description binding site for residue ACP B 301
source : AC4

7) chain B
residue 38
type
sequence A
description binding site for residue ACP B 301
source : AC4

8) chain B
residue 40
type
sequence K
description binding site for residue ACP B 301
source : AC4

9) chain B
residue 72
type
sequence V
description binding site for residue ACP B 301
source : AC4

10) chain B
residue 92
type
sequence M
description binding site for residue ACP B 301
source : AC4

11) chain B
residue 93
type
sequence E
description binding site for residue ACP B 301
source : AC4

12) chain B
residue 95
type
sequence V
description binding site for residue ACP B 301
source : AC4

13) chain B
residue 99
type
sequence T
description binding site for residue ACP B 301
source : AC4

14) chain B
residue 145
type
sequence M
description binding site for residue ACP B 301
source : AC4

15) chain B
residue 156
type
sequence D
description binding site for residue MG B 302
source : AC5

16) chain B
residue 17
type MOD_RES
sequence L
description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160
source Swiss-Prot : SWS_FT_FI2

17) chain B
residue 40
type MOD_RES
sequence K
description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160
source Swiss-Prot : SWS_FT_FI2

18) chain B
residue 93
type MOD_RES
sequence E
description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160
source Swiss-Prot : SWS_FT_FI2

19) chain B
residue 140
type MOD_RES
sequence K
description Phosphothreonine; by PknG => ECO:0000269|PubMed:19019160
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 143
type MOD_RES
sequence N
description Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616
source Swiss-Prot : SWS_FT_FI3

21) chain B
residue 156
type MOD_RES
sequence D
description Phosphothreonine; by PknB => ECO:0000269|PubMed:15978616
source Swiss-Prot : SWS_FT_FI3

22) chain B
residue 2
type MOD_RES
sequence T
description N-acetylthreonine => ECO:0007744|PubMed:21969609
source Swiss-Prot : SWS_FT_FI4

23) chain B
residue 169
type MOD_RES
sequence S
description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283
source Swiss-Prot : SWS_FT_FI6

24) chain B
residue 171
type MOD_RES
sequence X
description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609, ECO:0000269|PubMed:19008858
source Swiss-Prot : SWS_FT_FI7

25) chain B
residue 173
type MOD_RES
sequence X
description Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609
source Swiss-Prot : SWS_FT_FI8


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