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Crystal structure of cold-adapted chitinase from moritella marina with a reaction product - NAG2

Analyse Crystal structure of cold-adapted chitinase from moritella marina with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HME
Type: protein
Length: 528 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase 60
EC: 3.2.1.14
UniProt: B1VBB0
Ligands: NAG, NA
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase 60 (EC 3.2.1.14)	protein	528	24% helix, 29% strand	B1VBB0

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
NA · Sodium ion · metal · chains A
GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	271	0.58	0.78	34	empty
2	203	0.54	0.78	32	NAG
3	117	0.40	0.76	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4HME · Crystal structure of cold-adapted chitinase from Moritella marina with a reaction product… · 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 B1VBB0
Elsewhere: RCSB PDB 4HME · PDBe 4HME · UniProt B1VBB0

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