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Choline binding domain of the major autolysin (C-lyta) from streptococcus pneumoniae

Analyse Choline binding domain of the major autolysin (C-lyta) from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HCX
Type: protein
Length: 254 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major autolysin
EC: 3.5.1.28
UniProt: P06653
Ligands: CHT, DDQ, TPT

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Major autolysin (EC 3.5.1.28)	protein	127	0% helix, 38% strand	P06653

Ligands and binding sites

CHT · Choline ion · ligand · 5 copies · chains A, B
DDQ · Decylamine-N,N-dimethyl-N-oxide · ligand · 2 copies · chains B
TPT · 2,2':6',2''-TERPYRIDINE PLATINUM(II) Chloride · ligand · chains A

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

Interfaces

1 interface between chains.

A–B · 1014 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1HCX · Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae · the same entry in another collection · chain A against A, TM-score 1.00
P06653 · AlphaFold monomer V2.0 prediction for autolysin (P06653) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 P06653
Elsewhere: RCSB PDB 1HCX · PDBe 1HCX · UniProt P06653

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