MolNFT v1 · #103619 · protein

Structure of the double-stranded DNA binding type IV secretion protein tran from enterococcus

4PM3 · AM32: “Structure of the double-stranded DNA binding type IV secretion protein tran from enterococcus”. X-ray diffraction, 2 ligands (PT, BR), 1 pocket (best druggability 0.60). MolNFT v1 #103619 on GenesisL1: 3D structure, binding…

PDB: 4PM3
Type: protein
Length: 227 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AM32
UniProt: Q7BVV5
Ligands: PT, BR
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AM32	protein	112	46% helix, 21% strand	Q7BVV5
B	AM32	protein	115	44% helix, 21% strand	Q7BVV5

Ligands and binding sites

PT · Platinum (II) ion · metal · 2 copies · chains A, B
BR · Bromide ion · ion · 4 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	486	0.60	0.75	45	empty

Interfaces

1 interface between chains.

A–B · 314 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4PM3 · Structure of the double-stranded DNA binding type IV secretion protein TraN from… · 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 Q7BVV5
Elsewhere: RCSB PDB 4PM3 · PDBe 4PM3 · UniProt Q7BVV5

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