1ZQ9

Crystal structure of human Dimethyladenosine transferase

PDB DOI: https://doi.org/10.2210/pdb1ZQ9/pdb

Classification: TRANSFERASE
Organism(s): Homo sapiens
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2005-05-18 Released: 2005-05-31
Deposition Author(s): Dong, A., Wu, H., Zeng, H., Loppnau, P., Sundstrom, M., Arrowsmith, C., Edwards, A., Bochkarev, A., Plotnikov, A., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 ?
R-Value Free: 0.235
R-Value Work: 0.164
R-Value Observed: 0.165

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

Crystal structure of human Dimethyladenosine transferase with SAM

Wu, H., Dong, A., Zeng, H., Loppnau, P., Sundstrom, M., Arrowsmith, C., Edwards, A., Bochkarev, A., Plotnikov, A.

To be published.

Macromolecule Content

Total Structure Weight: 64.89 kDa
Atom Count: 5,281
Modelled Residue Count: 556
Deposited Residue Count: 570
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Probable dimethyladenosine transferase	A, B	285	Homo sapiens	Mutation(s): 0 EC: 2.1.1 (PDB Primary Data), 2.1.1.183 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for Q9UNQ2 (Homo sapiens) Explore Q9UNQ2 Go to UniProtKB: Q9UNQ2
PHAROS: Q9UNQ2 GTEx: ENSG00000086189
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9UNQ2
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SAM Query on SAM Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B] mmCIF format, chain C [auth A] mmCIF format, chain D [auth B]	C [auth A], D [auth B]	S-ADENOSYLMETHIONINE C₁₅ H₂₂ N₆ O₅ S MEFKEPWMEQBLKI-FCKMPRQPSA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 ?
R-Value Free: 0.235
R-Value Work: 0.164
R-Value Observed: 0.165
Space Group: P 1 2₁ 1

Unit Cell:

Length ( ? )	Angle ( ? )
a = 39.629	α = 90
b = 185.243	β = 91.3
c = 45.072	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
ADSC	data collection
SCALEPACK	data scaling
SOLVE	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2005-05-31

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2005-05-31
Type: Initial release
Version 1.1: 2008-04-30
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-02-14
Changes: Data collection, Database references, Derived calculations

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Deposit Data

Help and Resources

1ZQ9

Crystal structure of human Dimethyladenosine transferase

Crystal structure of human Dimethyladenosine transferase with SAM

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)