Structure of PDB 3hiv Chain A

Receptor sequence
>3hivA (length=257) Species: 3572 (Saponaria officinalis) [Search protein sequence]
VIIYELNLQGTTKAQYSTFLKQLRDDIKDPNLHYGGTNLPVIKRPVGPPK
FLRVNLKASTGTVSLAVQRSNLYVAAYLAKNNNKQFRAYYFKGFQITTNQ
LNNLFPEATGVSNQQELGYGESYPQIQNAAGVTRQQAGLGIKKLAESMTK
VNGVARVEKDEALFLLIVVQMVGEAARFKYIENLVLNNFDTAKEVEPVPD
RVIILENNWGLLSRAAKTANNGVFQTPLVLTSYAVPGVEWRVTTVAEVEI
GIFLNVD
3D structure
PDB3hiv Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins.
ChainA
Resolution2.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V74 E174 R177
Catalytic site (residue number reindexed from 1) V74 E174 R177
Enzyme Commision number 3.2.2.22: rRNA N-glycosylase.
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 TXN A N71 Y73 V74 E121 Y123 E174 R177 E206 N207 W209 G210 R214 L254 N71 Y73 V74 E121 Y123 E174 R177 E206 N207 W209 G210 R214 L254 MOAD: Ki=7.5nM
PDBbind-CN: -logKd/Ki=8.12,Ki=7.5nM
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0030598 rRNA N-glycosylase activity
GO:0090729 toxin activity
Biological Process
GO:0006952 defense response
GO:0017148 negative regulation of translation
GO:0035821 modulation of process of another organism

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Molecular Function
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Biological Process
External links
PDB RCSB:3hiv, PDBe:3hiv, PDBj:3hiv
PDBsum3hiv
PubMed19920175
UniProtQ2QEH4

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