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Crystal structure analysis of human S100A13

Analyse Crystal structure analysis of human S100A13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H2K
Type: protein
Length: 186 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein S100-A13
UniProt: Q99584
Ligands: CA

Structure

x-ray diffraction · 2 distinct chains · 60% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein S100-A13	protein	93	61% helix, 4% strand	Q99584
B	Protein S100-A13	protein	93	59% helix, 4% strand	Q99584

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 1699 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

2H2K · Crystal Structure Analysis of Human S100A13 · the same entry in another collection · chain A against A, TM-score 1.00
Q99584 · AlphaFold monomer V2.0 prediction for protein S100-A13 (Q99584) · a predicted model of the same protein · chain A against A, TM-score 0.86

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q99584
Elsewhere: RCSB PDB 2H2K · PDBe 2H2K · UniProt Q99584

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