Structure of PDB 4ruh Chain A

Receptor sequence

>4ruhA (length=458) Species: 9606 (Homo sapiens)

LTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVK
QLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQ
PAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQE
IPVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKK
PCITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDK
RGNILIPGINEDIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLH
GIEGAFSGSGAKTVIPRKVVGKFSIRLVPNMTPEVVGEQVTSYLTKKFAE
LRSPNEFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGS
IPVTLTFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYL
YEVSQLKD

3D structure

• PDB: 4ruh Crystal structure of Human Carnosinase-2 (CN2) in complex with inhibitor, Bestatin at 2.25 A
• Chain: A
• Resolution: 2.25 Å

Enzymatic activity

• Enzyme Commision number: 3.4.13.18: cytosol non-specific dipeptidase.

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	BES	A	H99 E166 E167 D195 L210 R343 H380 E414 G416 S417 H445	H96 E163 E164 D192 L207 R326 H363 E397 G399 S400 H428
BS02	MN	A	H99 D132 D195	H96 D129 D192
BS03	MN	A	D132 E167 H445	D129 E164 H428
BS04	BES	A	H228 T330	H225 T313

Gene Ontology

Molecular Function

• GO:0004180 carboxypeptidase activity
• GO:0005515 protein binding
• GO:0008233 peptidase activity
• GO:0008237 metallopeptidase activity
• GO:0016787 hydrolase activity
• GO:0016805 dipeptidase activity
• GO:0046872 metal ion binding
• GO:0070573 metallodipeptidase activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005654 nucleoplasm
• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:4ruh, PDBe:4ruh, PDBj:4ruh
• PDBsum: 4ruh
• UniProt: Q96KP4|CNDP2_HUMAN Cytosolic non-specific dipeptidase (Gene Name=CNDP2)