9O4E | pdb_00009o4e

EcAvs2 bound to phage PhiV-1 terminase


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.33 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Starting Model: in silico
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wwPDB Validation 3D Report Full Report

Validation slider image for 9O4E

This is version 1.0 of the entry. See complete history

Literature

Structural basis of phage terminase recognition by the bacterial immune receptor Avs2

Chiu, C.Evans, S.A.Wilkinson, M.E.Li, D.Zhang, F.Gao, A.

To be published.

Macromolecule Content 

  • Total Structure Weight: 965.12 kDa 
  • Atom Count: 52,496 
  • Modeled Residue Count: 6,292 
  • Deposited Residue Count: 8,280 
  • Unique protein chains: 2

Macromolecules

Find similar proteins by:|  3D Structure
Entity ID: 1
MoleculeChains  Sequence LengthOrganismDetailsImage
AVAST type 2 anti-phage system protein Avs2
A, B, C, D
1,484Escherichia coliMutation(s): 0 
Find similar proteins by:|  3D Structure
Entity ID: 2
MoleculeChains  Sequence LengthOrganismDetailsImage
Terminase, large subunit
E, F, G, H
586Escherichia phage PhiV-1Mutation(s): 0 
EC: 3.6.4 (PDB Primary Data), 3.1.21 (PDB Primary Data)
UniProt
Find proteins for A0A7G3WWS0 (Escherichia phage PhiV-1)
Explore A0A7G3WWS0 
Go to UniProtKB:  A0A7G3WWS0
Entity Groups
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A7G3WWS0
Sequence Annotations
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Reference Sequence

Small Molecules

Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ATP
(Subject of Investigation/LOI)

Query on ATP



Download:Ideal Coordinates CCD File
CA [auth E]
EA [auth F]
GA [auth G]
I [auth A]
IA [auth H]
CA [auth E],
EA [auth F],
GA [auth G],
I [auth A],
IA [auth H],
J [auth A],
N [auth B],
O [auth B],
S [auth C],
T [auth C],
X [auth D],
Y [auth D]
ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
MG
(Subject of Investigation/LOI)

Query on MG



Download:Ideal Coordinates CCD File
AA [auth D]
BA [auth D]
DA [auth E]
FA [auth F]
HA [auth G]
AA [auth D],
BA [auth D],
DA [auth E],
FA [auth F],
HA [auth G],
JA [auth H],
K [auth A],
L [auth A],
M [auth A],
P [auth B],
Q [auth B],
R [auth B],
U [auth C],
V [auth C],
W [auth C],
Z [auth D]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N

Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.33 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION4.0
MODEL REFINEMENTCoot
MODEL REFINEMENTISOLDE
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History 

& Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Other privateUnited States--

Revision History  (Full details and data files)

  • Version 1.0: 2026-05-06
    Type: Initial release