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Crystal structure of human peptidoglycan recognition protein (pgrp-S)

Analyse Crystal structure of human peptidoglycan recognition protein (pgrp-S) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YCK
Type: protein
Length: 167 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidoglycan recognition protein
UniProt: O75594
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidoglycan recognition protein	protein	167	31% helix, 20% strand	O75594

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	68	0.29	0.73	24	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1YCK · Crystal structure of human peptidoglycan recognition protein (PGRP-S) · the same entry in another collection · chain A against A, TM-score 1.00
O75594 · AlphaFold monomer V2.0 prediction for peptidoglycan recognition protein 1 (O75594) · 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 O75594
Elsewhere: RCSB PDB 1YCK · PDBe 1YCK · UniProt O75594

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