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Crystal structure of engineered HIV-1 reverse transcriptase RNase H domain complexed with nitrofuran METHOXY(METHOXYCARBONYL)PHENYL ester

Analyse Crystal structure of engineered HIV-1 reverse transcriptase RNase H domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7XIS
Type: protein
Length: 145 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Reverse transcriptase RNase H domain
EC: 3.1.26.13
UniProt: A0A059PIR4, A0A7L9QW77
Ligands: E58, MN, ZN
Pockets: 1 · best druggability 0.24

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Reverse transcriptase RNase H domain (EC 3.1.26.13)	protein	145	33% helix, 23% strand	A0A059PIR4, A0A7L9QW77

Ligands and binding sites

E58 · (2-methoxy-4-methoxycarbonyl-phenyl) 5-nitrofuran-2-carboxylate · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
ZN · Zinc ion · metal · 2 copies · 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	0.24	0.73	14	E58

Compared structures

7XIS · Crystal structure of engineered HIV-1 Reverse Transcriptase RNase H domain complexed with… · 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 A0A059PIR4
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Elsewhere: RCSB PDB 7XIS · PDBe 7XIS · UniProt A0A059PIR4 · UniProt A0A7L9QW77

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