Structure of PDB 1yi9 Chain A Binding Site BS01
Receptor Information
>1yi9 Chain A (length=295) Species:
10116
(Rattus norvegicus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
CLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVID
FKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAP
PTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRV
PQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHL
GKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFT
GEEICNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIP
Ligand information
Ligand ID
CU
InChI
InChI=1S/Cu/q+2
InChIKey
JPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Cu+2]
CACTVS 3.341
[Cu++]
Formula
Cu
Name
COPPER (II) ION
ChEMBL
DrugBank
DB14552
ZINC
PDB chain
1yi9 Chain A Residue 357 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1yi9
The catalytic copper of Peptidylglycine alpha-Hydroxylating Monooxygenase also plays a critical structural role.
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
H108 H172
Binding residue
(residue number reindexed from 1)
H62 H126
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H107 H108 Q170 H172 H242 H244 I314
Catalytic site (residue number reindexed from 1)
H61 H62 Q124 H126 H196 H198 I254
Enzyme Commision number
1.14.17.3
: peptidylglycine monooxygenase.
4.3.2.5
: peptidylamidoglycolate lyase.
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0004497
monooxygenase activity
GO:0005507
copper ion binding
GO:0016715
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
Biological Process
GO:0006518
peptide metabolic process
Cellular Component
GO:0016020
membrane
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1yi9
,
PDBe:1yi9
,
PDBj:1yi9
PDBsum
1yi9
PubMed
16100265
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
[
Back to BioLiP
]