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Crystal structure of human GRP78 (70KDA heat shock protein 5 / bip) ATPase domain in apo form

Analyse Crystal structure of human GRP78 (70KDA heat shock protein 5 / bip) ATPase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LDN
Type: protein
Length: 764 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 78 kda glucose-regulated protein
UniProt: P11021
Pockets: 8 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	78 kda glucose-regulated protein	protein	382	41% helix, 27% strand	P11021

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	623	0.75	0.82	63	empty
2	282	0.74	0.87	48	empty
3	869	0.71	0.76	71	empty
4	394	0.68	0.81	41	empty
5	142	0.45	0.76	24	empty

Interfaces

1 interface between chains.

A–B · 300 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3LDN · Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo… · the same entry in another collection · chain A against A, TM-score 1.00
P11021 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (P11021) · a predicted model of the same protein · chain B against A, TM-score 0.88

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 P11021
Elsewhere: RCSB PDB 3LDN · PDBe 3LDN · UniProt P11021

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