Structure of PDB 4ryc Chain B

Receptor sequence
>4rycB (length=336) Species: 9606 (Homo sapiens) [Search protein sequence]
TLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKC
SRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGG
ITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQG
VLKEDVFSFYYNRDSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQ
MKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFD
YVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMD
IPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
3D structure
PDB4ryc trans-(3S,4S)-Disubstituted pyrrolidines as inhibitors of the human aspartyl protease renin. Part I: Prime site exploration using an amino linker.
ChainB
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 N37 W39 Y75 D215 A218
Catalytic site (residue number reindexed from 1) D37 S40 N42 W44 Y82 D222 A225
Enzyme Commision number 3.4.23.15: renin.
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 3ZK B T12 Q13 Y14 V30 D32 G34 Y75 S76 P111 L114 A115 F117 Q128 L213 D215 G217 A218 T295 T17 Q18 Y19 V35 D37 G39 Y82 S83 P117 L120 A121 F123 Q134 L220 D222 G224 A225 T305 MOAD: ic50=0.08uM
BindingDB: IC50=80nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ryc, PDBe:4ryc, PDBj:4ryc
PDBsum4ryc
PubMed25782742
UniProtP00797|RENI_HUMAN Renin (Gene Name=REN)

[Back to BioLiP]