Research workbench

PVHL54-213-elob-eloc COMPLEX_APO

Analyse PVHL54-213-elob-eloc COMPLEX_APO in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZRF
Type: protein
Length: 1,325 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription elongation factor B polypeptide 2; Transcription elongation factor B…
UniProt: Q15370, Q15369, P40337
Pockets: 9 · best druggability 0.64

Structure

x-ray diffraction · 9 distinct chains · 27% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription elongation factor B polypeptide 2	protein	101	18% helix, 37% strand	Q15370
B, H	Transcription elongation factor B polypeptide 1	protein	86	49% helix, 15% strand	Q15369
C, F	Von hippel-lindau disease tumor suppressor,	protein	142	21% helix, 30% strand	P40337
D	Transcription elongation factor B polypeptide 2	protein	98	15% helix, 37% strand	Q15370
E	Transcription elongation factor B polypeptide 1	protein	87	45% helix, 15% strand	Q15369
G, J	Transcription elongation factor B polypeptide 2	protein	105	14% helix, 32% strand	Q15370
I	Von hippel-lindau disease tumor suppressor,	protein	145	23% helix, 28% strand	P40337
K	Transcription elongation factor B polypeptide 1	protein	85	47% helix, 13% strand	Q15369
L	Von hippel-lindau disease tumor suppressor,	protein	143	24% helix, 29% strand	P40337

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.64	0.79	44	empty
2	280	0.60	0.79	40	empty
3	156	0.56	0.82	30	empty
4	161	0.45	0.75	26	empty
5	68	0.42	0.80	17	empty

Interfaces

18 interfaces between chains.

G–H · 1139 Å² buried · 17 hydrogen bonds · protein-protein
J–K · 1108 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1092 Å² buried · 14 hydrogen bonds · protein-protein
D–E · 1079 Å² buried · 12 hydrogen bonds · protein-protein
H–I · 1069 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3ZRF · pVHL54-213-EloB-EloC complex_apo · the same entry in another collection · chain L against L, TM-score 1.00

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 Q15370
Every structure of UniProt Q15369
Every structure of UniProt P40337
Elsewhere: RCSB PDB 3ZRF · PDBe 3ZRF · UniProt Q15370 · UniProt Q15369 · UniProt P40337

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