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Crystal structure determination of a putative NADH-dependent reductase using sulfur anomalous signal

Analyse Crystal structure determination of a putative NADH-dependent reductase using… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RTT
Type: protein
Length: 174 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Conserved hypothetical protein
UniProt: Q9I4D4
Ligands: SO4
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Conserved hypothetical protein	protein	174	39% helix, 19% strand	Q9I4D4

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.28	0.75	14	empty

Compared structures

1RTT · Crystal structure determination of a putative NADH-dependent reductase using sulfur… · the same entry in another collection · chain A against A, TM-score 1.00
Q9I4D4 · AlphaFold monomer V2.0 prediction for NAD(P)H-dependent FMN reductase PA1204 (Q9I4D4) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9I4D4
Elsewhere: RCSB PDB 1RTT · PDBe 1RTT · UniProt Q9I4D4

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