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Crystal structure of putative hydrolase (YP_002548124.1) from agrobacterium vitis S4 at 1.80 a resolution

Analyse Crystal structure of putative hydrolase (YP_002548124.1) from agrobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LLC
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative hydrolase
UniProt: B9JYM4
Ligands: CL
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative hydrolase	protein	261	38% helix, 23% strand	B9JYM4

Ligands and binding sites

CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
PG4 · Tetraethylene glycol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	459	0.69	0.80	37	CL, PG4
2	60	0.31	0.75	14	EDO

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3LLC · Crystal structure of Putative hydrolase (YP_002548124.1) from Agrobacterium vitis S4 at… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B9JYM4
Elsewhere: RCSB PDB 3LLC · PDBe 3LLC · UniProt B9JYM4

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