Structure of PDB 3hu2 Chain B

Receptor sequence
>3hu2B (length=452) Species: 9606 (Homo sapiens) [Search protein sequence]
LSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKG
KKRREAVCIVLSDDTCSDEKIRMNAVVRNNLRVRLGDVISIQPCPDVKYG
KRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAV
EFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRK
QLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANE
TGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAP
KREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG
RFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADL
AALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNP
SA
3D structure
PDB3hu2 A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants.
ChainB
Resolution2.85 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.6: vesicle-fusing ATPase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AGS B R359 F360 R348 F349 PDBbind-CN: -logKd/Ki=7.22,Kd=0.06uM
BS02 AGS B I206 G207 P247 G248 T249 G250 K251 T252 L253 N348 H384 G408 A409 I195 G196 P236 G237 T238 G239 K240 T241 L242 N337 H373 G397 A398 PDBbind-CN: -logKd/Ki=7.22,Kd=0.06uM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity

View graph for
Molecular Function
External links
PDB RCSB:3hu2, PDBe:3hu2, PDBj:3hu2
PDBsum3hu2
PubMed20512113
UniProtP55072|TERA_HUMAN Transitional endoplasmic reticulum ATPase (Gene Name=VCP)

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