Structure of PDB 5fch Chain B Binding Site BS01
Receptor Information
>5fch Chain B (length=395) Species:
190485
(Xanthomonas campestris pv. campestris str. ATCC 33913) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
STQIGGMSLDQARTQLAPWTQRAAPIGADEYQQRIERARVLMRAQGVDAL
LIGAGTSLRYFSGVPWGASERLVALLLTTEGDPVLICPAFEEGSLDAVLQ
LPVRKRLWEEHEDPYALVVQAMDEQHAHALALDPGIAFAVHTGLRAHLGT
AIRDAGAIIDGCRMCKSPAELALMQQACDMTLLVQRLAAGIAHEGIGTDQ
LVRFIDEAHRALGADNGSTFCIVQFGHATAFPHGVQHLRAGELVLIDTGC
TVQGYHSDITRTWIYGTPSDAQQRIWELELAAQAAAFAAVRPGVACEAVD
QAARAVLQAAGLGPDYRLPGLPHRTGHGCGLAIHEAPYLVRGNRQPLQPG
MCASNEPMIVVPGAFGVRLEDHFYVTDTGAQWFTPPSVAIDQPFA
Ligand information
>5fch Chain C (length=3) Species:
562
(Escherichia coli) [
Search peptide sequence
] [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
GGG
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
5fch
Crystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases
Resolution
1.95 Å
Binding residue
(original residue number in PDB)
H142 R146 I153
Binding residue
(residue number reindexed from 1)
H141 R145 I152
Enzymatic activity
Catalytic site (original residue number in PDB)
H234 D251 D262 T264 H327 H331 H338 E360 V364 R372 E374
Catalytic site (residue number reindexed from 1)
H233 D247 D258 T260 H323 H327 H334 E356 V360 R368 E370
Enzyme Commision number
3.4.13.9
: Xaa-Pro dipeptidase.
Gene Ontology
Molecular Function
GO:0046872
metal ion binding
View graph for
Molecular Function
External links
PDB
RCSB:5fch
,
PDBe:5fch
,
PDBj:5fch
PDBsum
5fch
PubMed
27816563
UniProt
Q8P839
[
Back to BioLiP
]