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Crystal structure of the bovine lactadherin C2 domain

Analyse Crystal structure of the bovine lactadherin C2 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PQS
Type: protein
Length: 636 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lactadherin
UniProt: Q95114
Pockets: 3 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Lactadherin	protein	159	8% helix, 48% strand	Q95114

Pockets

3 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	125	0.40	0.75	23	empty
2	126	0.39	0.74	22	empty
3	62	0.28	0.73	15	empty

Interfaces

3 interfaces between chains.

C–D · 456 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 452 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 11 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

2PQS · Crystal Structure of the Bovine Lactadherin C2 Domain · the same entry in another collection · chain A against A, TM-score 1.00
Q95114 · AlphaFold monomer V2.0 prediction for lactadherin (Q95114) · 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 Q95114
Elsewhere: RCSB PDB 2PQS · PDBe 2PQS · UniProt Q95114

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