Structure of PDB 6zmd Chain A

Receptor sequence
>6zmdA (length=523) Species: 9606 (Homo sapiens) [Search protein sequence]
GSGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERL
IGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTK
PYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAY
FNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDL
GGGAFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTG
KDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRA
KFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLV
KEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLG
IETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKD
NHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKIT
ITNDQNRLTPEEIERMVNDAEKF
3D structure
PDB6zmd Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD.
ChainA
Resolution2.64 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone 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 ANP A G36 T37 T38 Y39 K96 E201 G226 G227 G228 A229 E293 K296 R297 S300 G363 G364 R367 G11 T12 T13 Y14 K71 E176 G201 G202 G203 A204 E268 K271 R272 S275 G338 G339 R342
BS02 MG A D34 Y39 D9 Y14
BS03 MG A E201 D224 E176 D199
BS04 PO4 A R101 T102 D105 H477 R76 T77 D80 H452
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0140662 ATP-dependent protein folding chaperone

View graph for
Molecular Function
External links
PDB RCSB:6zmd, PDBe:6zmd, PDBj:6zmd
PDBsum6zmd
PubMed33893288
UniProtP11021|BIP_HUMAN Endoplasmic reticulum chaperone BiP (Gene Name=HSPA5)

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