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The crystal structure of oxidoreductase from marinobacter aquaeolei

Analyse The crystal structure of oxidoreductase from marinobacter aquaeolei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3RH9
Type: protein
Length: 957 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Succinate-semialdehyde dehydrogenase (NAD(P)(+))
EC: 1.2.1.16
UniProt: A1U6U7
Pockets: 8 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Succinate-semialdehyde dehydrogenase (NAD(P)(+)) (EC 1.2.1.16)	protein	481	41% helix, 20% strand	A1U6U7
B	Succinate-semialdehyde dehydrogenase (NAD(P)(+)) (EC 1.2.1.16)	protein	476	41% helix, 20% strand	A1U6U7

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1011	0.84	0.85	105	empty
2	578	0.71	0.80	75	empty
3	447	0.63	0.77	54	empty
4	118	0.60	0.85	24	empty
5	167	0.55	0.80	32	empty

Interfaces

1 interface between chains.

A–B · 2747 Å² buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 28 modified (engineered).

Compared structures

3RH9 · The crystal structure of oxidoreductase from Marinobacter aquaeolei · 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 A1U6U7
Elsewhere: RCSB PDB 3RH9 · PDBe 3RH9 · UniProt A1U6U7

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