- PDB-2oux: Crystal structure of the soluble part of a magnesium transporter -
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Basic information
Entry
Database: PDB / ID: 2oux
Title
Crystal structure of the soluble part of a magnesium transporter
Components
Magnesium transporter
Keywords
TRANSPORT PROTEIN / Magnesium transporter / 10001b / Structural Genomics / PSI-2 / Protein Structure Initiative / NYSGXRC / New York SGX Research Center for Structural Genomics
Function / homology
Function and homology information
magnesium ion transmembrane transporter activity / membrane => GO:0016020 / metal ion binding / plasma membrane Similarity search - Function
: / MgtE N-terminal fold / MgtE N-terminal domain-like / MgtE, N-terminal domain superfamily / SLC41A/MgtE, integral membrane domain / Magnesium transporter, MgtE intracellular domain / Magnesium transporter MgtE / SLC41A/MgtE divalent cation transporters, integral membrane domain superfamily / Divalent cation transporter / MgtE intracellular N domain ...: / MgtE N-terminal fold / MgtE N-terminal domain-like / MgtE, N-terminal domain superfamily / SLC41A/MgtE, integral membrane domain / Magnesium transporter, MgtE intracellular domain / Magnesium transporter MgtE / SLC41A/MgtE divalent cation transporters, integral membrane domain superfamily / Divalent cation transporter / MgtE intracellular N domain / MgtE intracellular N domain / CBS-domain / CBS-domain / Domain in cystathionine beta-synthase and other proteins. / CBS domain / CBS domain / CBS domain profile. / Alpha Horseshoe / Roll / Mainly Alpha / Alpha Beta Similarity search - Domain/homology
Resolution: 2.1→2.18 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.527 / Mean I/σ(I) obs: 20 / % possible all: 57.9
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Processing
Software
Name
Version
Classification
CNS
1.1
refinement
CBASS
datacollection
HKL-2000
datareduction
HKL-2000
datascaling
SHELXD
phasing
SHARP
phasing
ARP/wARP
modelbuilding
Refinement
Method to determine structure: SAD / Resolution: 2.16→38.61 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 125321.76 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: Missing residues listed in 465 are due to lack of electron density
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