MolNFT v1 · #111985 · protein

Structural and biochemical characterization of a non-functionally redundant M. tuberculosis (3,3) L,D-transpeptidase, LDTMT5.

4Z7A · Mycobacterium tuberculosis (3,3)L,D-transpeptidase type 5: “Structural and biochemical characterization of a non-functionally redundant M. tuberculosis (3,3)…”. X-ray diffraction, 2 ligands (ACE, PO4), 2 pockets (best druggability…

PDB: 4Z7A
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mycobacterium tuberculosis (3,3)L,D-transpeptidase type 5
UniProt: A5TZL1
Ligands: ACE, PO4
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mycobacterium tuberculosis (3,3)L,D-transpeptidase type 5	protein	355	9% helix, 43% strand	A5TZL1

Ligands and binding sites

ACE · Acetyl group · ligand · chains A
PO4 · Phosphate ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A
PGE · Triethylene glycol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.41	0.80	23	empty
2	53	0.25	0.72	14	empty

Compared structures

4Z7A · Structural and biochemical characterization of a non-functionally redundant M.… · 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 A5TZL1
Elsewhere: RCSB PDB 4Z7A · PDBe 4Z7A · UniProt A5TZL1

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