Structure of PDB 4ruh Chain B

Receptor sequence

>4ruhB (length=453) Species: 9606 (Homo sapiens)

LTTLFKYIDENQDRYIKKLAKWVAIQSVSAWPEKRGEIRRMMEVAAADVK
QLGGSVELVDIGKQKLPDGSEIPLPPILLGRLGSDPQKKTVCIYGHLDVQ
PAALEDGWDSEPFTLVERDGKLYGRGSTDDKGPVAGWINALEAYQKTGQE
IPVNVRFCLEGMEESGSEGLDELIFARKDTFFKDVDYVCISDNYWLGKKP
CITYGLRGICYFFIEVECSNKDLHSGVYGGSVHEAMTDLILLMGSLVDKR
GNILIPGIIDFDIEEFAKDVGAQILLHSHKKDILMHRWRYPSLSLHGIEG
AFSGSGAKTVIPRKVVGKFSIRLVPMTPEVVGEQVTSYLTKKFAELRSPN
EFKVYMGHGGKPWVSDFSHPHYLAGRRAMKTVFGVEPDLTREGGSIPVTL
TFQEATGKNVMLLPVGSADDGAHSQNEKLNRYNYIEGTKMLAAYLYEVSQ
LKD

3D structure

• PDB: 4ruh Crystal structure of Human Carnosinase-2 (CN2) in complex with inhibitor, Bestatin at 2.25 A
• Chain: B
• 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	B	H228 T330	H224 T309
BS02	BES	B	D132 E166 E167 D195 Y197 I213 R343 E414 G416 S417 H445	D129 E163 E164 D192 Y194 I209 R322 E392 G394 S395 H423
BS03	MN	B	H99 D132 D195	H96 D129 D192
BS04	MN	B	D132 E167 H445	D129 E164 H423

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)