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C. crescentus mreb, monomeric, amppnp

Analyse C. crescentus mreb, monomeric, amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CZM
Type: protein
Length: 672 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rod shape-determining protein mreb
UniProt: B8H609
Ligands: ANP, MG
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Rod shape-determining protein mreb	protein	336	41% helix, 29% strand	B8H609

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	927	0.83	0.85	111	MG, ANP
2	410	0.73	0.84	62	MG, ANP
3	55	0.30	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 942 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4CZM · C. crescentus MreB, monomeric, AMPPNP · 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 B8H609
Elsewhere: RCSB PDB 4CZM · PDBe 4CZM · UniProt B8H609

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