Research workbench

K38H mutant of streptomyces K15 dd-transpeptidase

Analyse K38H mutant of streptomyces K15 dd-transpeptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J9M
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dd-transpeptidase
EC: 3.4.16.4
UniProt: P39042
Ligands: NA, CL
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dd-transpeptidase (EC 3.4.16.4)	protein	257	39% helix, 24% strand	P39042

Ligands and binding sites

NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · chains A

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

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	77	0.31	0.74	24	empty

Compared structures

1J9M · K38H mutant of Streptomyces K15 DD-transpeptidase · the same entry in another collection · chain A against A, TM-score 1.00
P39042 · AlphaFold monomer V2.0 prediction for D-alanyl-D-alanine carboxypeptidase (P39042) · a predicted model of the same protein · 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 P39042
Elsewhere: RCSB PDB 1J9M · PDBe 1J9M · UniProt P39042

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