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Human psoriasin (S100A7)

Analyse Human psoriasin (S100A7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PSR
Type: protein
Length: 200 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Psoriasin
UniProt: P31151
Ligands: HO
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Psoriasin	protein	100	61% helix, 2% strand	P31151

Ligands and binding sites

HO · Holmium atom · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	149	0.65	0.86	28	empty
2	111	0.43	0.77	20	empty
3	68	0.35	0.77	20	empty

Interfaces

1 interface between chains.

A–B · 1244 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1PSR · Human psoriasin (S100A7) · the same entry in another collection · chain A against A, TM-score 1.00
P31151 · AlphaFold monomer V2.0 prediction for protein S100-A7 (P31151) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P31151
Elsewhere: RCSB PDB 1PSR · PDBe 1PSR · UniProt P31151

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