2MYS

MYOSIN SUBFRAGMENT-1, ALPHA CARBON COORDINATES ONLY FOR THE TWO LIGHT CHAINS

PDB DOI: https://doi.org/10.2210/pdb2MYS/pdb
Entry: 2MYS supersedes: 1MYS

Classification: MUSCLE PROTEIN
Organism(s): Gallus gallus
Mutation(s): Yes

Deposited: 1996-06-27 Released: 1997-01-11
Deposition Author(s): Rayment, I., Holden, H.M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Work: 0.223

wwPDB Validation 3D Report Full Report

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

Literature

Three-dimensional structure of myosin subfragment-1: a molecular motor.

Rayment, I., Rypniewski, W.R., Schmidt-Base, K., Smith, R., Tomchick, D.R., Benning, M.M., Winkelmann, D.A., Wesenberg, G., Holden, H.M.

(1993) Science 261: 50-58

PubMed: 8316857 Search on PubMed
DOI: https://doi.org/10.1126/science.8316857
Primary Citation of Related Structures:
2MYS

PubMed Abstract:
Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.

Organizational Affiliation

Department of Biochemistry, University of Wisconsin, Madison 53705.

Macromolecule Content

Total Structure Weight: 131.67 kDa
Atom Count: 6,788
Modelled Residue Count: 1,072
Deposited Residue Count: 1,158
Unique protein chains: 3

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
MYOSIN	A	843	Gallus gallus	Mutation(s): 44
UniProt
Find proteins for P13538 (Gallus gallus) Explore P13538 Go to UniProtKB: P13538
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P13538
Sequence Annotations Expand
Reference Sequence

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
MYOSIN	B	166	Gallus gallus	Mutation(s): 0
UniProt
Find proteins for P02609 (Gallus gallus) Explore P02609 Go to UniProtKB: P02609
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P02609
Sequence Annotations Expand
Reference Sequence

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 3
Molecule	Chains	Sequence Length	Organism	Details	Image
MYOSIN	C	149	Gallus gallus	Mutation(s): 0
UniProt
Find proteins for P02604 (Gallus gallus) Explore P02604 Go to UniProtKB: P02604
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P02604
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A] mmCIF format, chain D [auth A]	D [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain D [auth A]
MG Query on MG Download Ideal Coordinates CCD File SDF format, chain E [auth B] MOL2 format, chain E [auth B] mmCIF format, chain E [auth B]	E [auth B]	MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N		Interactions Focus chain E [auth B]

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MLY Query on MLY	A	L-PEPTIDE LINKING	C₈ H₁₈ N₂ O₂		LYS

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Work: 0.223
Space Group: C 2 2 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 98.4	α = 90
b = 124.2	β = 90
c = 274.9	γ = 90

Software Package:

Software Name	Purpose
TNT	refinement
XDS	data reduction
ROSSMANN	data reduction
CCP4	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1997-01-11

Deposition Author(s):

Rayment, I.

Holden, H.M.

This entry supersedes: 1MYS

Revision History (Full details and data files)

Version 1.0: 1997-01-11
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-06-05
Changes: Data collection, Database references, Derived calculations, Other