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Structure of H-2DB with truncated sev peptide and gl

Analyse Structure of H-2DB with truncated sev peptide and gl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GB5
Type: protein
Length: 765 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P01899, P01887
Ligands: SO4

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	274	—	P01899
B, D	—	protein	99	—	P01887
C	—	protein	275	—	P01899
E, F	—	protein	7	—	—
G, H	—	protein	2	—	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, C
GOL · Glycerol · additive · 3 copies · chains A, C, D

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

Compared structures

6GB5 · Structure of H-2Db with truncated SEV peptide and GL · the same entry in another collection · chain F against F, TM-score 1.00
P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain D against A, TM-score 0.98

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 P01899
Every structure of UniProt P01887
Elsewhere: RCSB PDB 6GB5 · PDBe 6GB5 · UniProt P01899 · UniProt P01887

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