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Crystal structure of NADH-dependent reductase A1-R' responsible for alginate metabolism

Analyse Crystal structure of NADH-dependent reductase A1-R' responsible for alginate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TKL
Type: protein
Length: 486 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NADH-dependent reductase for 4-deoxy-L-erythro-5- hexoseulose uronate
Ligands: PO4
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADH-dependent reductase for 4-deoxy-L-erythro-5- hexoseulose uronate	protein	246	51% helix, 17% strand	—
B	NADH-dependent reductase for 4-deoxy-L-erythro-5- hexoseulose uronate	protein	240	50% helix, 16% strand	—

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, B

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

Pockets

2 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	385	0.58	0.76	45	PO4
2	283	0.53	0.75	47	PO4

Interfaces

1 interface between chains.

A–B · 1471 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4TKL · Crystal structure of NADH-dependent reductase A1-R' responsible for alginate metabolism · 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
Elsewhere: RCSB PDB 4TKL · PDBe 4TKL

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