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Crystal structure of cbpb from streptococcus agalactiae

Analyse Crystal structure of cbpb from streptococcus agalactiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZZ9
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cbs domain-containing protein
UniProt: A0A076YWK5
Ligands: PT, SO4
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cbs domain-containing protein	protein	160	45% helix, 23% strand	A0A076YWK5
B	Cbs domain-containing protein	protein	158	44% helix, 23% strand	A0A076YWK5

Ligands and binding sites

PT · Platinum (II) ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	632	0.69	0.77	53	SO4

Interfaces

1 interface between chains.

A–B · 1806 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6ZZ9 · Crystal structure of CbpB from Streptococcus agalactiae · 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 A0A076YWK5
Elsewhere: RCSB PDB 6ZZ9 · PDBe 6ZZ9 · UniProt A0A076YWK5

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