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Full-length replication protein a subunits RPA14 and RPA32

Analyse Full-length replication protein a subunits RPA14 and RPA32 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PI2
Type: protein
Length: 972 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replication protein a 32 kda subunit; Replication protein a 14 kda subunit
UniProt: P15927, P35244
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 7 distinct chains · 21% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replication protein a 32 kda subunit	protein	129	20% helix, 47% strand	P15927
B	Replication protein a 32 kda subunit	protein	124	21% helix, 48% strand	P15927
C	Replication protein a 32 kda subunit	protein	125	20% helix, 44% strand	P15927
D	Replication protein a 32 kda subunit	protein	123	21% helix, 47% strand	P15927
E, H	Replication protein a 14 kda subunit	protein	117	21% helix, 34% strand	P35244
F	Replication protein a 14 kda subunit	protein	119	21% helix, 34% strand	P35244
G	Replication protein a 14 kda subunit	protein	118	21% helix, 34% strand	P35244

Ligands and binding sites

DIO · 1,4-diethylene dioxide · additive · 4 copies · chains A, E, B, F, C, G, D, H

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	720	0.73	0.78	53	empty
2	236	0.62	0.81	25	empty
3	97	0.49	0.81	19	empty
4	149	0.46	0.77	21	empty
5	100	0.37	0.75	22	empty

Interfaces

8 interfaces between chains.

B–F · 1359 Å² buried · 16 hydrogen bonds · protein-protein
C–G · 1345 Å² buried · 17 hydrogen bonds · protein-protein
A–E · 1325 Å² buried · 15 hydrogen bonds · protein-protein
D–H · 1294 Å² buried · 16 hydrogen bonds · protein-protein
E–H · 380 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2PI2 · Full-length Replication protein A subunits RPA14 and RPA32 · the same entry in another collection · chain E against E, TM-score 1.00
P15927 · AlphaFold monomer V2.0 prediction for replication protein a 32 kda subunit (P15927) · a predicted model of the same protein · chain D against A, TM-score 0.98
P35244 · AlphaFold monomer V2.0 prediction for replication protein a 14 kda subunit (P35244) · a predicted model of the same protein · chain E against A, TM-score 0.98

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 P15927
Every structure of UniProt P35244
Elsewhere: RCSB PDB 2PI2 · PDBe 2PI2 · UniProt P15927 · UniProt P35244

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