9LRQ | pdb_00009lrq

Indole monooxygenase from Acinetobacter baumannii


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 
    0.217 (Depositor), 0.217 (DCC) 
  • R-Value Work: 
    0.177 (Depositor), 0.178 (DCC) 
  • R-Value Observed: 
    0.179 (Depositor) 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.0 of the entry. See complete history


Literature

Structure and reaction mechanisms of a two-component indole monooxygenase from Acinetobacter baumannii.

Suksomjaisaman, K.Thananon, K.Mangkalee, M.Thotsaporn, K.Tinikul, R.Schulte, A.Wangkanon, K.Sirikantaramas, S.Sucharitakul, J.Chaiyen, P.

(2025) Arch Biochem Biophys : 110681


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alanine-phosphoribitol ligase
A, B, C, D
420Acinetobacter baumanniiMutation(s): 0 
UniProt
Find proteins for A0A088D986 (Acinetobacter baumannii)
Explore A0A088D986 
Go to UniProtKB:  A0A088D986
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A088D986
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free:  0.217 (Depositor), 0.217 (DCC) 
  • R-Value Work:  0.177 (Depositor), 0.178 (DCC) 
  • R-Value Observed: 0.179 (Depositor) 
Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.287α = 65.19
b = 82.427β = 80.08
c = 93.43γ = 79.15
Software Package:
Software NamePurpose
PHENIXrefinement
MOSFLMdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Other governmentThailandChulalongkorn University

Revision History  (Full details and data files)

  • Version 1.0: 2025-12-10
    Type: Initial release