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Crystal structure of alpha-neoagarobiose hydrolase (alpha-nabh) from saccharophagus degradans 2-40

Analyse Crystal structure of alpha-neoagarobiose hydrolase (alpha-nabh) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3R4Y
Type: protein
Length: 719 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl hydrolase family 32, N terminal
EC: 3.2.1.-
UniProt: Q21HB2
Pockets: 7 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl hydrolase family 32, N terminal (EC 3.2.1.-)	protein	360	4% helix, 43% strand	Q21HB2
B	Glycosyl hydrolase family 32, N terminal (EC 3.2.1.-)	protein	359	6% helix, 43% strand	Q21HB2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	135	0.80	0.97	31	empty
2	149	0.79	0.96	31	empty
3	440	0.69	0.81	60	empty
4	161	0.48	0.77	22	empty
5	148	0.46	0.77	23	empty

Interfaces

1 interface between chains.

A–B · 3299 Å² buried · 47 hydrogen bonds · protein-protein

Compared structures

3R4Y · Crystal structure of alpha-neoagarobiose hydrolase (ALPHA-NABH) from Saccharophagus… · 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 Q21HB2
Elsewhere: RCSB PDB 3R4Y · PDBe 3R4Y · UniProt Q21HB2

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