Structure of PDB 3mid Chain A Binding Site BS04
Receptor Information
>3mid Chain A (length=311) Species:
10116
(Rattus norvegicus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
NECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFV
IDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARN
APPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLT
RVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTH
HLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCV
FTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFR
TIPAEANIPIP
Ligand information
Ligand ID
AZI
InChI
InChI=1S/N3/c1-3-2/q-1
InChIKey
IVRMZWNICZWHMI-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[N-]=[N+]=[N-]
Formula
N3
Name
AZIDE ION
ChEMBL
CHEMBL79455
DrugBank
ZINC
PDB chain
3mid Chain A Residue 4 [
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
3mid
Differential Reactivity Between the Two Copper Sites of Peptidylglycine alpha-Hydroxylating Monooxygenase (PHM)
Resolution
3.06 Å
Binding residue
(original residue number in PDB)
R256 N257 I288
Binding residue
(residue number reindexed from 1)
R212 N213 I244
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H107 H108 Q170 H172 H242 H244 M314
Catalytic site (residue number reindexed from 1)
H63 H64 Q126 H128 H198 H200 M270
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:3mid
,
PDBe:3mid
,
PDBj:3mid
PDBsum
3mid
PubMed
20958070
UniProt
P14925
|AMD_RAT Peptidylglycine alpha-amidating monooxygenase (Gene Name=Pam)
[
Back to BioLiP
]