Structure of PDB 1xd3 Chain C

Receptor sequence

>1xd3C (length=227) Species: 9606 (Homo sapiens)

QRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVL
LLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHA
IANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAH
EGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLE
DAIEVCKKFMERDPDELRFNAIALSAA

3D structure

• PDB: 1xd3 Structure of the Ubiquitin Hydrolase UCH-L3 Complexed with a Suicide Substrate
• Chain: C
• Resolution: 1.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q89 C95 H169 D184
• Catalytic site (residue number reindexed from 1): Q86 C92 H166 D181
• Enzyme Commision number: 3.4.19.12: ubiquitinyl hydrolase 1.

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	MG	C	Q78 D79	Q75 D76
BS02	MG	C	D79 V80	D76 V77
BS03	GVE	C	N93 C95 V166 L168 H169	N90 C92 V163 L165 H166

Gene Ontology

Molecular Function

• GO:0004843 cysteine-type deubiquitinase activity
• GO:0005515 protein binding
• GO:0008233 peptidase activity
• GO:0008234 cysteine-type peptidase activity
• GO:0019784 deNEDDylase activity
• GO:0043130 ubiquitin binding

Biological Process

• GO:0006508 proteolysis
• GO:0006511 ubiquitin-dependent protein catabolic process
• GO:0016567 protein ubiquitination
• GO:0016579 protein deubiquitination
• GO:0030163 protein catabolic process
• GO:0043687 post-translational protein modification

Cellular Component

• GO:0005654 nucleoplasm
• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1xd3, PDBe:1xd3, PDBj:1xd3
• PDBsum: 1xd3
• PubMed: 15531586
• UniProt: P15374|UCHL3_HUMAN Ubiquitin carboxyl-terminal hydrolase isozyme L3 (Gene Name=UCHL3)