2D64

Aspartate Aminotransferase Mutant MABC With Isovaleric Acid

PDB DOI: https://doi.org/10.2210/pdb2D64/pdb

Classification: TRANSFERASE
Organism(s): Escherichia coli
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2005-11-09 Released: 2006-11-14
Deposition Author(s): Tanaka, Y., Nakagawa, N., Tada, H., Yano, T., Masui, R., Kuramitsu, S.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.05 ?
R-Value Free: 0.231
R-Value Work: 0.194
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.3 of the entry. See complete history.

Literature

The Structures of Aspartate Aminotransferase with Mutations of Non-Active-Site Residues

Tanaka, Y., Nakagawa, N., Tada, H., Yano, T., Masui, R., Kuramitsu, S.

To be published.

Macromolecule Content

Total Structure Weight: 43.94 kDa
Atom Count: 3,334
Modelled Residue Count: 396
Deposited Residue Count: 396
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Aspartate aminotransferase	A	396	Escherichia coli	Mutation(s): 14 Gene Names: aspC EC: 2.6.1.1 (PDB Primary Data), 2.6.1 (UniProt)
UniProt
Find proteins for Q304P7 (Escherichia coli) Explore Q304P7 Go to UniProtKB: Q304P7
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q304P7
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PLP Query on PLP Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	PYRIDOXAL-5'-PHOSPHATE C₈ H₁₀ N O₆ P NGVDGCNFYWLIFO-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]
IVA Query on IVA Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A] mmCIF format, chain C [auth A]	C [auth A]	ISOVALERIC ACID C₅ H₁₀ O₂ GWYFCOCPABKNJV-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.05 ?
R-Value Free: 0.231
R-Value Work: 0.194
R-Value Observed: 0.194
Space Group: C 2 2 2₁

Unit Cell:

Length ( ? )	Angle ( ? )
a = 156.712	α = 90
b = 84.862	β = 90
c = 78.514	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
DENZO	data reduction
SCALEPACK	data scaling
AMoRE	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2006-11-14

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2006-11-14
Type: Initial release
Version 1.1: 2008-04-30
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Derived calculations, Version format compliance
Version 1.3: 2021-11-10
Changes: Database references, Derived calculations

Prepare Data

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Deposit Data

Help and Resources

2D64

Aspartate Aminotransferase Mutant MABC With Isovaleric Acid

The Structures of Aspartate Aminotransferase with Mutations of Non-Active-Site Residues

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)