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3-D solution structure of reduced apo-S100B from rat, NMR, 20 structures

Analyse 3-D solution structure of reduced apo-S100B from rat, NMR, 20 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SYM
Type: protein
Length: 184 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S100B
UniProt: P04631
Pockets: 2 · best druggability 0.29

Structure

solution nmr · 1 distinct chain · 60% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	S100B	protein	92	60% helix, 4% strand	P04631

Pockets

2 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	60	0.29	0.74	12	empty
2	57	0.28	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 1694 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1SYM · 3-D solution structure of reduced apo-S100B from rat, NMR, 20 structures · the same entry in another collection · chain B against B, TM-score 1.00
P04631 · AlphaFold monomer V2.0 prediction for protein S100-B (P04631) · a predicted model of the same protein · chain A against A, TM-score 0.61

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 P04631
Elsewhere: RCSB PDB 1SYM · PDBe 1SYM · UniProt P04631

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