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R248L mutant of streptomyces K15 dd-transpeptidase

Analyse R248L 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: 1ESI
Type: protein
Length: 260 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

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dd-transpeptidase (EC 3.4.16.4)	protein	260	39% helix, 23% strand	P39042

Compared structures

1ESI · R248L 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 0.99

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 1ESI · PDBe 1ESI · UniProt P39042

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