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Structure of a cysteine synthase (O-acetylserine sulfhydrylase (oass)) from mycobacterium marinum atcc baa-535 / M

Analyse Structure of a cysteine synthase (O-acetylserine sulfhydrylase (oass)) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3RR2
Type
protein
Length
291 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cysteine synthase
EC
2.5.1.47
UniProt
B2HL85
Pockets
1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACysteine synthase (EC 2.5.1.47)protein29140% helix, 19% strandB2HL85

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17880.700.7681empty

Compared structures

  • 3RR2 · Structure of a Cysteine synthase (O-Acetylserine Sulfhydrylase (OASS)) from Mycobacterium… · the same entry in another collection · chain A against A, TM-score 1.00

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