Structure of PDB 3l6c Chain B Binding Site BS02
Receptor Information
>3l6c Chain B (length=312) Species:
10116
(Rattus norvegicus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
QYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTG
SFKIRGALNAIRGPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPN
CKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAG
QGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPS
NADDCYQSKLKGELTPNLHPPETIADGVKSSIGLNTWPIIRDLVDDVFTV
TEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPEVKNICIVL
SGGNVDLTSLSW
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
3l6c Chain B Residue 340 [
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
3l6c
The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
E210 A214 D216
Binding residue
(residue number reindexed from 1)
E198 A202 D204
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
K56 S84 E210 A214 D216 G239 T285 L312 S313
Catalytic site (residue number reindexed from 1)
K53 S72 E198 A202 D204 G227 T273 L300 S301
Enzyme Commision number
4.3.1.17
: L-serine ammonia-lyase.
4.3.1.18
: D-serine ammonia-lyase.
5.1.1.18
: serine racemase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0003824
catalytic activity
GO:0003941
L-serine ammonia-lyase activity
GO:0005509
calcium ion binding
GO:0005524
ATP binding
GO:0008721
D-serine ammonia-lyase activity
GO:0016594
glycine binding
GO:0016829
lyase activity
GO:0016853
isomerase activity
GO:0018114
threonine racemase activity
GO:0030165
PDZ domain binding
GO:0030170
pyridoxal phosphate binding
GO:0030378
serine racemase activity
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
Biological Process
GO:0006520
amino acid metabolic process
GO:0006563
L-serine metabolic process
GO:0009069
serine family amino acid metabolic process
GO:0009410
response to xenobiotic stimulus
GO:0014070
response to organic cyclic compound
GO:0032496
response to lipopolysaccharide
GO:0042866
pyruvate biosynthetic process
GO:0070178
D-serine metabolic process
GO:0070179
D-serine biosynthetic process
Cellular Component
GO:0005737
cytoplasm
GO:0043025
neuronal cell body
GO:0045177
apical part of cell
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:3l6c
,
PDBe:3l6c
,
PDBj:3l6c
PDBsum
3l6c
PubMed
20106978
UniProt
Q76EQ0
|SRR_RAT Serine racemase (Gene Name=Srr)
[
Back to BioLiP
]