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Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76 ångströms resolution

Analyse Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BRN
Type: protein + DNA
Length: 222 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'-D(*CP*GP*AP*C)-3'); Protein (barnase (E.C.3.1.27.-))
EC: 3.1.27.-
UniProt: P00648
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	DNA (5'-D(CPGPAPC)-3')	dna	3	—	—
L, M	Protein (barnase (E.C.3.1.27.-)) (EC 3.1.27.-)	protein	108	22% helix, 23% strand	P00648

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	68	0.28	0.73	24	empty

Interfaces

6 interfaces between chains.

B–M · 534 Å² buried · 25 hydrogen bonds · protein-nucleic
A–L · 528 Å² buried · 25 hydrogen bonds · protein-nucleic
L–M · 228 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 138 Å² buried · 8 hydrogen bonds · nucleic-nucleic
A–M · 82 Å² buried · 0 hydrogen bonds · protein-nucleic

Compared structures

1BRN · Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76… · the same entry in another collection · chain M against M, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00648
Elsewhere: RCSB PDB 1BRN · PDBe 1BRN · UniProt P00648

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