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Avpf bound to BIR3-xiap

Analyse Avpf bound to BIR3-xiap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OPZ
Type: protein
Length: 452 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Baculoviral iap repeat-containing protein 4; Avpf (smac homologue, N-terminal…
UniProt: P98170
Ligands: ZN

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Baculoviral iap repeat-containing protein 4	protein	109	50% helix, 8% strand	P98170
E, F, G, H	Avpf (smac homologue, N-terminal tetrapeptide)	protein	4	0% helix, 50% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

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

Interfaces

7 interfaces between chains.

A–C · 505 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 472 Å² buried · 5 hydrogen bonds · protein-protein
B–F · 354 Å² buried · 7 hydrogen bonds · protein-protein
A–E · 350 Å² buried · 7 hydrogen bonds · protein-protein
C–G · 347 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2OPZ · AVPF bound to BIR3-XIAP · the same entry in another collection · chain A against A, 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 P98170
Elsewhere: RCSB PDB 2OPZ · PDBe 2OPZ · UniProt P98170

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