Research workbench

Homo sapiens S100A5

Analyse Homo sapiens S100A5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WN7
Type: protein
Length: 536 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein S100-A5
UniProt: P33763
Ligands: CA
Pockets: 4 · best druggability 0.38

Structure

x-ray diffraction · 5 distinct chains · 64% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein S100-A5	protein	87	62% helix, 2% strand	P33763
B, D	Protein S100-A5	protein	90	68% helix, 2% strand	P33763
C	Protein S100-A5	protein	90	61% helix, 2% strand	P33763
F	Protein S100-A5	protein	88	68% helix, 5% strand	P33763
E	Protein S100-A5	protein	91	60% helix, 2% strand	P33763

Ligands and binding sites

CA · Calcium ion · metal · 18 copies · chains A, B, C, D, F, E

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

Pockets

4 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	141	0.38	0.73	30	CA
2	97	0.38	0.76	19	empty
3	86	0.30	0.72	17	empty
4	56	0.28	0.74	15	empty

Interfaces

8 interfaces between chains.

F–E · 1462 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 1396 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 1376 Å² buried · 9 hydrogen bonds · protein-protein
C–E · 209 Å² buried · 3 hydrogen bonds · protein-protein
C–F · 164 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6WN7 · Homo sapiens S100A5 · the same entry in another collection · chain E against E, TM-score 1.00
P33763 · AlphaFold monomer V2.0 prediction for protein S100-A5 (P33763) · a predicted model of the same protein · chain F 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 P33763
Elsewhere: RCSB PDB 6WN7 · PDBe 6WN7 · UniProt P33763

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