6H2O

APO structure of Phenylalanine ammonia-lyase from Petroselinum crispum

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 

wwPDB Validation   3D Report Full Report


This is version 2.1 of the entry. See complete history. 


Literature

Substrate Tunnel Engineering Aided by X-ray Crystallography and Functional Dynamics Swaps the Function of MIO-Enzymes

Bata, Z., Molnar, Z., Madaras, E., Molnar, B., Santa-Bell, E., Varga, A., Leveles, I., Qian, R., Hammerschmidt, F., Paizs, C., Vertessy, B.G., Poppe, L.

(2021) ACS Catal : 4538-4549


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phenylalanine ammonia-lyase 1
A, B
714Petroselinum crispumMutation(s): 3 
Gene Names: PAL1
EC: 4.3.1.24
UniProt
Find proteins for P24481 (Petroselinum crispum)
Explore P24481 
Go to UniProtKB:  P24481
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24481
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MDO
Query on MDO
A, B
L-PEPTIDE LINKINGC8 H11 N3 O3ALA, SER, GLY
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 119.89α = 90
b = 161.12β = 90
c = 141.43γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
PHENIXphasing

Structure Validation

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View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
National Research Development and Innovation Office (NKFIH)HungaryK119493
National Research Development and Innovation Office (NKFIH)HungaryNVKP_16-1-2016-0020
National Research Development and Innovation Office (NKFIH)Hungary2017-1.3.1-VKE-2017-00002
National Research Development and Innovation Office (NKFIH)Hungary2017-1.3.1-VKE-2017-00013
National Research Development and Innovation Office (NKFIH)HungaryVEKOP-2.3.2-16-2017-00013
National Research Development and Innovation Office (NKFIH)HungaryNKP-2018-1.2.1-NKP-2018-00005
Ministry of Human CapacitiesHungaryBME FIKP-BIO
Hungarian Academy of SciencesHungaryMedinProt grant
Ministry of Human CapacitiesHungaryUNKP-2017-3-III
National Authority for Scientific Research in Romania (ANCS)RomaniaID P_37_273, Cod MySMIS 103413
National Research Development and Innovation Office (NKFIH)HungarySNN-125637

Revision History  (Full details and data files)

  • Version 1.0: 2019-07-31
    Type: Initial release
  • Version 1.1: 2021-04-14
    Changes: Database references
  • Version 1.2: 2021-04-28
    Changes: Author supporting evidence, Data collection, Refinement description
  • Version 2.0: 2023-11-15
    Changes: Atomic model, Data collection, Database references, Derived calculations, Refinement description
  • Version 2.1: 2024-01-17
    Changes: Refinement description