Structure of PDB 2zep Chain B

Receptor sequence
>2zepB (length=320) Species: 9606 (Homo sapiens) [Search protein sequence]
ASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSP
GSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAK
RHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLK
PDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQL
HGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHS
LEGRYFQNYSYIQDDHIPFLRRGVPVLLLIPSPFPEVWHTMDDNEENLDE
STIDNLNKILQVFVLEYLHL
3D structure
PDB2zep A conserved hydrogen-bond network in the catalytic centre of animal glutaminyl cyclases is critical for catalysis.
ChainB
Resolution2.1 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 2.3.2.5: glutaminyl-peptide cyclotransferase.
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 B D159 E202 H330 D127 E164 H289
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016603 glutaminyl-peptide cyclotransferase activity
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0017186 peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
GO:0036211 protein modification process
Cellular Component
GO:0005576 extracellular region
GO:0035580 specific granule lumen
GO:0070062 extracellular exosome
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2zep, PDBe:2zep, PDBj:2zep
PDBsum2zep
PubMed18072935
UniProtQ16769|QPCT_HUMAN Glutaminyl-peptide cyclotransferase (Gene Name=QPCT)

[Back to BioLiP]