2ZWR

Crystal structure of TTHA1623 from thermus thermophilus HB8


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8

Yamamura, A.Okada, A.Kameda, Y.Ohtsuka, J.Nakagawa, N.Ebihara, A.Nagata, K.Tanokura, M.

(2009) Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 455-459

  • DOI: https://doi.org/10.1107/S174430910901361X
  • Primary Citation of Related Structures:  
    2ZWR, 2ZZI

  • PubMed Abstract: 

    TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape.


  • Organizational Affiliation

    Department of Applied Biological Chemistry, University of Tokyo, Yayoi, Bunkyo-ku, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Metallo-beta-lactamase superfamily protein
A, B
207Thermus thermophilus HB8Mutation(s): 0 
Gene Names: TTHA1623
UniProt
Find proteins for Q5SHV7 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SHV7 
Go to UniProtKB:  Q5SHV7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SHV7
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
C [auth A]
D [auth A]
E [auth A]
F [auth A]
G [auth A]
C [auth A],
D [auth A],
E [auth A],
F [auth A],
G [auth A],
H [auth A],
I [auth A],
J [auth A],
K [auth B],
L [auth B],
M [auth B],
N [auth B],
O [auth B],
P [auth B]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.190 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.136α = 90
b = 114.122β = 90
c = 114.711γ = 90
Software Package:
Software NamePurpose
SOLVEphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-10-06
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references, Derived calculations