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Crystal structure of the SAMD1 SAM domain

Analyse Crystal structure of the SAMD1 SAM domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LUJ
Type: protein
Length: 330 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Atherin
UniProt: Q6SPF0
Ligands: SO4

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Atherin	protein	66	65% helix, 0% strand	Q6SPF0

Ligands and binding sites

SO4 · Sulfate ion · ion · 16 copies · chains A, C, B, E, D

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

Interfaces

5 interfaces between chains.

C–D · 526 Å² buried · 8 hydrogen bonds · protein-protein
B–E · 511 Å² buried · 8 hydrogen bonds · protein-protein
A–E · 506 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 498 Å² buried · 11 hydrogen bonds · protein-protein
A–C · 495 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6LUJ · Crystal structure of the SAMD1 SAM domain · the same entry in another collection · chain A against A, TM-score 1.00
Q6SPF0 · AlphaFold monomer V2.0 prediction for atherin (Q6SPF0) · 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 Q6SPF0
Elsewhere: RCSB PDB 6LUJ · PDBe 6LUJ · UniProt Q6SPF0

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