MolNFT v1 · #191318 · protein

The complex of GTF2B peptide tgaasfdef presented by H2-kd

8D5E: “The complex of GTF2B peptide tgaasfdef presented by H2-kd”. X-ray diffraction. MolNFT v1 #191318 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 8D5E
Type: protein
Length: 382 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P01900, P01887, P62915

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	274	—	P01900
B	—	protein	99	—	P01887
P	—	protein	9	—	P62915

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Compared structures

8D5E · The complex of Gtf2b Peptide TGAASFDEF Presented by H2-Dd · the same entry in another collection · chain A against A, TM-score 1.00
P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain B against A, TM-score 0.99
P01900 · AlphaFold monomer V2.0 prediction for H-2 class I histocompatibility antigen, D-D alpha… · a predicted model of the same protein · chain A against A, TM-score 0.97
P62915 · AlphaFold monomer V2.0 prediction for transcription initiation factor iib (P62915) · a predicted model of the same protein · chain P against A, TM-score 0.44

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 P01900
Every structure of UniProt P01887
Every structure of UniProt P62915
Elsewhere: RCSB PDB 8D5E · PDBe 8D5E · UniProt P01900 · UniProt P01887 · UniProt P62915

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