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Crystal structure of porcine heart mitochondrial complex II bound with 2-iodo-N-phenyl-benzamide

Analyse Crystal structure of porcine heart mitochondrial complex II bound with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AED
Type: protein
Length: 1,092 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; Succinate…
EC: 1.3.5.1
UniProt: Q0QF01, Q007T0, D0VWV4, A5GZW8
Ligands: FAD, FES, SF4, F3S, HEM, BOL, EPH
Pockets: 15 · best druggability 0.86

Structure

x-ray diffraction · 4 distinct chains · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1)	protein	613	33% helix, 19% strand	Q0QF01
B	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1)	protein	239	30% helix, 14% strand	Q007T0
C	Succinate dehydrogenase cytochrome B560 subunit, mitochondrial	protein	138	74% helix, 1% strand	D0VWV4
D	Succinate dehydrogenase [ubiquinone] cytochrome B small subunit, mitochondrial	protein	102	86% helix, 0% strand	A5GZW8

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A, B
FES · Fe2/s2 (inorganic) cluster · ligand · chains B
SF4 · Iron/sulfur cluster · ligand · chains B
F3S · FE3-S4 cluster · ligand · chains B
HEM · Protoporphyrin IX containing Fe · ligand · chains B, C, D
BOL · 2-iodo-N-phenylbenzamide · ligand · chains B, C, D
EPH · L-alpha-phosphatidyl-beta-oleoyl-gamma-palmitoyl-phosphatidylethanolamine · ligand · chains C, D
MLI · Malonate ion · additive · chains A

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

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	315	0.86	0.96	57	FAD, MLI
2	1065	0.85	0.86	92	HEM, BOL, EPH
3	92	0.75	0.96	19	empty
4	381	0.69	0.81	36	empty
5	386	0.65	0.79	34	empty

Interfaces

5 interfaces between chains.

A–B · 2802 Å² buried · 48 hydrogen bonds · protein-protein
B–C · 1762 Å² buried · 17 hydrogen bonds · protein-protein
C–D · 1340 Å² buried · 9 hydrogen bonds · protein-protein
B–D · 660 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 115 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3AED · Crystal structure of porcine heart mitochondrial complex II bound with… · the same entry in another collection · chain D against D, TM-score 1.00
Q0QF01 · AlphaFold monomer V2.0 prediction for succinate dehydrogenase [ubiquinone] flavoprotein… · a predicted model of the same protein · chain A against A, TM-score 1.00
Q007T0 · AlphaFold monomer V2.0 prediction for succinate dehydrogenase [ubiquinone] iron-sulfur… · a predicted model of the same protein · chain B against A, TM-score 0.99
A5GZW8 · AlphaFold monomer V2.0 prediction for succinate dehydrogenase [ubiquinone] cytochrome B… · a predicted model of the same protein · chain D against A, TM-score 0.99
D0VWV4 · AlphaFold monomer V2.0 prediction for succinate dehydrogenase cytochrome B560 subunit… · a predicted model of the same protein · chain C against A, TM-score 0.93

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 Q0QF01
Every structure of UniProt Q007T0
Every structure of UniProt D0VWV4
Every structure of UniProt A5GZW8
Elsewhere: RCSB PDB 3AED · PDBe 3AED · UniProt Q0QF01 · UniProt Q007T0 · UniProt D0VWV4 · UniProt A5GZW8

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