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Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with 2'-deoxy-ATP

X-ray diffraction
1.86Å resolution
PDB entry 5ey4 coloured by chain, front view.
PDB entry 5ey4 coloured by chain, side view.
PDB entry 5ey4 coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Endoplasmic reticulum chaperone BiP
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Multimeric state: monomeric
Accessible surface area: 17164.88 Å2
Buried surface area: 641.01 Å2
Dissociation area: 320.5 Å2
Dissociation energy (ΔGdiss): -3.48 kcal/mol
Dissociation entropy (TΔSdiss): 5.2 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145633
Assembly 2
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Assembly Name: Endoplasmic reticulum chaperone BiP
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Multimeric state: monomeric
Accessible surface area: 17624.9 Å2
Buried surface area: 537.31 Å2
Dissociation area: 268.65 Å2
Dissociation energy (ΔGdiss): -5.95 kcal/mol
Dissociation entropy (TΔSdiss): 5.26 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145633

Macromolecules

Endoplasmic reticulum chaperone BiP
Chains: A, B
Length: 400 amino acids
Theoretical weight: 44.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11021 (Residues: 26-407; Coverage: 60%)
Gene names: GRP78, HSPA5
Pfam: Hsp70 protein
InterPro:
CATH:
Endoplasmic reticulum chaperone BiP in PDB entry 5ey4, assembly 1, front view.
Endoplasmic reticulum chaperone BiP in PDB entry 5ey4, assembly 1, side view.
Endoplasmic reticulum chaperone BiP in PDB entry 5ey4, assembly 1, top view.
PDBe-KB: UniProt Coverage View: P11021  
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