Structure of PDB 3dlj Chain A

Receptor sequence
>3dljA (length=471) Species: 9606 (Homo sapiens) [Search protein sequence]
PPPALLEKVFQYIDLHQDEFVQTLKEWVAIESDSVQPVPRFRQELFRMMA
VAADTLQRLGARVASVDMGPQQLGQSLPIPPVILAELGSDPTKGTVCFYG
HLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFR
ALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLW
ISKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSL
VDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDT
KEEILMHLWRYPSLSIHGIEGAFDEPGTKTVIPGRVIGKFSIRLVPHMNV
SAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKRA
IRTVFGTEPDMIRDGSTIPIAKMFQEIVHVVLIPLGAVDDGEHSQNEKIN
RWNYIEGTKLFAAFFLEMAQL
3D structure
PDB3dlj Crystal structure of human carnosine dipeptidase 1.
ChainA
Resolution2.26 Å
3D
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
Enzyme Commision number 3.4.13.20: beta-Ala-His 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 ZN A D139 E174 H452 D134 E169 H443
BS02 ZN A H106 D139 D202 H101 D134 D197
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0005515 protein binding
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
GO:0051246 regulation of protein metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3dlj, PDBe:3dlj, PDBj:3dlj
PDBsum3dlj
PubMed
UniProtQ96KN2|CNDP1_HUMAN Beta-Ala-His dipeptidase (Gene Name=CNDP1)

[Back to BioLiP]