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Complex of human CU,ZN SOD1 with the human copper chaperone for SOD1 in a compact conformation

Analyse Complex of human CU,ZN SOD1 with the human copper chaperone for SOD1 in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FP6
Type: protein
Length: 4,527 residues
Chains: 24
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superoxide dismutase [cu-zn]; Copper chaperone for superoxide dismutase
EC: 1.15.1.1
UniProt: P00441, O14618
Ligands: ZN
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 11 distinct chains · 11% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K, M, O, S, U, W	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	153	7% helix, 41% strand	P00441
B	Copper chaperone for superoxide dismutase	protein	231	12% helix, 39% strand	O14618
D	Copper chaperone for superoxide dismutase	protein	234	11% helix, 39% strand	O14618
F, L	Copper chaperone for superoxide dismutase	protein	234	12% helix, 38% strand	O14618
H	Copper chaperone for superoxide dismutase	protein	230	12% helix, 40% strand	O14618
J, R, X	Copper chaperone for superoxide dismutase	protein	232	14% helix, 40% strand	O14618
N	Copper chaperone for superoxide dismutase	protein	234	11% helix, 38% strand	O14618
P	Copper chaperone for superoxide dismutase	protein	231	12% helix, 39% strand	O14618
Q	Superoxide dismutase [cu-zn] (EC 1.15.1.1)	protein	151	3% helix, 38% strand	P00441
T	Copper chaperone for superoxide dismutase	protein	223	12% helix, 40% strand	O14618
V	Copper chaperone for superoxide dismutase	protein	146	5% helix, 42% strand	O14618

Ligands and binding sites

ZN · Zinc ion · metal · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
PPI · Propanoic acid · additive · 6 copies · chains A, J, I, G, K, N, R, S
GOL · Glycerol · additive · chains A

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	529	0.77	0.84	80	empty
2	293	0.76	0.89	45	empty
3	507	0.76	0.84	78	empty
4	514	0.75	0.83	54	empty
5	181	0.75	0.92	30	empty

Interfaces

45 interfaces between chains.

C–D · 1009 Å² buried · 12 hydrogen bonds · protein-protein
M–N · 1008 Å² buried · 13 hydrogen bonds · protein-protein
K–L · 1002 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 989 Å² buried · 11 hydrogen bonds · protein-protein
G–H · 972 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

6FP6 · Complex of human Cu,Zn SOD1 with the human copper chaperone for SOD1 in a compact… · the same entry in another collection · chain F against F, 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 P00441
Every structure of UniProt O14618
Elsewhere: RCSB PDB 6FP6 · PDBe 6FP6 · UniProt P00441 · UniProt O14618

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