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Crystal structure of BCAM1869 protein (rsam homolog) from burkholderia cenocepacia

Analyse Crystal structure of BCAM1869 protein (rsam homolog) from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4O2H
Type: protein
Length: 269 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein BCAM1869
UniProt: B4EMD1
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein BCAM1869	protein	137	33% helix, 33% strand	B4EMD1
B	Protein BCAM1869	protein	132	30% helix, 36% strand	B4EMD1

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	60	0.31	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 518 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

4O2H · Crystal structure of BCAM1869 protein (RsaM homolog) from Burkholderia cenocepacia · the same entry in another collection · chain A against A, 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 B4EMD1
Elsewhere: RCSB PDB 4O2H · PDBe 4O2H · UniProt B4EMD1

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