Research workbench

Rsc substrate-recruitment module

Analyse Rsc substrate-recruitment module in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6K15
Type: protein
Length: 2,655 residues
Chains: 13
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chromatin structure-remodeling complex subunit RSC7; Chromatin structure-remodeling…
EC: 3.6.4.12
UniProt: P32832, P43609, Q03124, P25632, Q06168, Q07979, P32597, Q9URQ5, P38781, Q06639, Q02206, Q06488
Ligands: ZN
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 13 distinct chains · 44% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F	Chromatin structure-remodeling complex subunit RSC7	protein	118	36% helix, 8% strand	P32832
H	Chromatin structure-remodeling complex protein RSC8	protein	393	52% helix, 6% strand	P43609
D	Chromatin structure-remodeling complex protein RSC8	protein	305	53% helix, 3% strand	P43609
M	Chromatin structure-remodeling complex subunit RSC9	protein	384	57% helix, 1% strand	Q03124
I	Chromatin structure-remodeling complex protein RSC6	protein	244	48% helix, 7% strand	P25632
G	Chromatin structure-remodeling complex subunit SFH1	protein	246	30% helix, 15% strand	Q06168
A	Chromatin structure-remodeling complex protein RSC58	protein	365	35% helix, 7% strand	Q07979
J	Nuclear protein STH1/NPS1 (EC 3.6.4.12)	protein	235	47% helix, 1% strand	P32597
E	High temperature lethal protein 1	protein	58	71% helix, 0% strand	Q9URQ5
C	Chromatin structure-remodeling complex protein RSC30	protein	33	64% helix, 12% strand	P38781
K	Chromatin structure-remodeling complex protein RSC3	protein	42	45% helix, 10% strand	Q06639
X	Chromatin structure-remodeling complex subunit RSC4	protein	147	10% helix, 37% strand	Q02206
L	Chromatin structure-remodeling complex subunit RSC2	protein	85	16% helix, 12% strand	Q06488

Ligands and binding sites

ZN · Zinc ion · metal · chains H, L

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	1070	0.84	0.85	119	empty
2	366	0.83	0.92	44	empty
3	555	0.83	0.88	66	empty
4	207	0.81	0.95	40	empty
5	251	0.81	0.93	31	empty

Interfaces

44 interfaces between chains.

A–J · 4651 Å² buried · 43 hydrogen bonds · protein-protein
H–D · 3696 Å² buried · 28 hydrogen bonds · protein-protein
H–I · 2876 Å² buried · 12 hydrogen bonds · protein-protein
A–L · 2825 Å² buried · 22 hydrogen bonds · protein-protein
H–G · 2814 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

6K15 · RSC substrate-recruitment module · the same entry in another collection · chain C against C, 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 P32832
Every structure of UniProt P43609
Every structure of UniProt Q03124
Every structure of UniProt P25632
Every structure of UniProt Q06168
Every structure of UniProt Q07979
Every structure of UniProt P32597
Every structure of UniProt Q9URQ5
Every structure of UniProt P38781
Every structure of UniProt Q06639
Every structure of UniProt Q02206
Every structure of UniProt Q06488
Elsewhere: RCSB PDB 6K15 · PDBe 6K15 · UniProt P32832 · UniProt P43609 · UniProt Q03124 · UniProt P25632 · UniProt Q06168 · UniProt Q07979 · UniProt P32597 · UniProt Q9URQ5 · UniProt P38781 · UniProt Q06639 · UniProt Q02206 · UniProt Q06488

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