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Crystal structure of the marine pl-14 alginate lyase from aplysia kurodai

Analyse Crystal structure of the marine pl-14 alginate lyase from aplysia kurodai in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GMT
Type: protein
Length: 528 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alginate lyase
EC: 4.2.2.3
UniProt: E7FLQ2
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alginate lyase (EC 4.2.2.3)	protein	267	9% helix, 44% strand	E7FLQ2
B	Alginate lyase (EC 4.2.2.3)	protein	261	9% helix, 49% strand	E7FLQ2

Pockets

5 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	758	0.71	0.77	81	empty
2	194	0.50	0.76	31	empty
3	54	0.35	0.78	15	empty
4	64	0.34	0.77	14	empty
5	50	0.33	0.79	15	empty

Interfaces

1 interface between chains.

A–B · 408 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5GMT · Crystal structure of the marine PL-14 alginate lyase from Aplysia kurodai · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt E7FLQ2
Elsewhere: RCSB PDB 5GMT · PDBe 5GMT · UniProt E7FLQ2

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