8UV4 | pdb_00008uv4

M. tuberculosis CTP synthase filament bound to substrates


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

M. tuberculosis CTP synthase filament bound to substrates

Lynch, E.M.Kollman, J.M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CTP synthase592Mycobacterium tuberculosisMutation(s): 0 
Gene Names: pyrG
EC: 6.3.4.2
UniProt
Find proteins for A0A045H225 (Mycobacterium tuberculosis)
Explore A0A045H225 
Go to UniProtKB:  A0A045H225
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A045H225
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
5ZL (Subject of Investigation/LOI)
Query on 5ZL

Download Ideal Coordinates CCD File 
AA [auth b]
CB [auth H]
DA [auth A]
GB [auth L]
HA [auth E]
AA [auth b],
CB [auth H],
DA [auth A],
GB [auth L],
HA [auth E],
LA [auth G],
N [auth R],
PA [auth K],
S [auth V],
TA [auth B],
X,
XA [auth F]
[[(2~{R},3~{S},4~{R},5~{R})-3,4-bis(oxidanyl)-5-(2-oxidanyl-4-phosphonooxy-pyrimidin-1-yl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate
C9 H17 N2 O18 P4
RYGLMDXZXSWNKW-XVFCMESISA-O
ADP (Subject of Investigation/LOI)
Query on ADP

Download Ideal Coordinates CCD File 
BB [auth H]
CA [auth A]
FB [auth L]
GA [auth E]
KA [auth G]
BB [auth H],
CA [auth A],
FB [auth L],
GA [auth E],
KA [auth G],
M [auth R],
OA [auth K],
R [auth V],
SA [auth B],
W [auth X],
WA [auth F],
Z [auth b]
ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
AB [auth H]
BA [auth b]
DB [auth H]
EA [auth A]
EB [auth L]
AB [auth H],
BA [auth b],
DB [auth H],
EA [auth A],
EB [auth L],
FA [auth A],
HB [auth L],
IA [auth E],
JA [auth E],
MA [auth G],
NA [auth G],
O [auth R],
P [auth R],
Q [auth R],
QA [auth K],
RA [auth K],
T [auth V],
U [auth V],
UA [auth B],
V,
VA [auth B],
Y [auth X],
YA [auth F],
ZA [auth F]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.20 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTISOLDE
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR35 GM149542

Revision History  (Full details and data files)

  • Version 1.0: 2025-07-02
    Type: Initial release