Structure of PDB 1mpx Chain B

Receptor sequence
>1mpxB (length=614) Species: 346 (Xanthomonas citri) [Search protein sequence]
TSPMTPDITGKPFVAADASNDYIKREVMIPMRDGVKLHTVIVLPKGAKNA
PIVLTRTPYDASGRTERLASPHMKDLLSAGDDVFVEGGYIRVFQDVRGKY
GSEGDYVMTRPLRGPLNPSEVDHATDAWDTIDWLVKNVSESNGKVGMIGS
SYEGFTVVMALTNPHPALKVAVPESPMIDGWMGDDWFNYGAFRQVNFDYF
TGQLSKRGKGAGIARQGHDDYSNFLQAGSAGDFAKAAGLEQLPWWHKLTE
HAAYDAFWQEQALDKVMARTPLKVPTMWLQGLWDQEDMWGAIHSYAAMEP
RDKRNTLNYLVMGPWRHSQVNYDGSALGALNFEGDTARQFRHDVLRPFFD
QYLVDGAPKADTPPVFIYNTGENHWDRLKAWPRSCDKGCAATSKPLYLQA
GGKLSFQPPVAGQAGFEEYVSDPAKPVPFVPRPVDFADRAMWTTWLVHDQ
RFVDGRPDVLTFVTEPLTEPLQIAGAPDVHLQASTSGSDSDWVVKLIDVY
PEEMASNPKMGGYELPVSLAIFRGRYRESFSTPKPLTSNQPLAFQFGLPT
ANHTFQPGHRVMVQVQSSLFPLYDRNPQTYVPNIFFAKPGDYQKATQRVY
VSPEQPSYISLPVR
3D structure
PDB1mpx The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y82 S174 Y175 Q226 D307 H340
Catalytic site (residue number reindexed from 1) Y59 S151 Y152 Q203 D284 H317
Enzyme Commision number 3.1.1.43: alpha-amino-acid esterase.
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 CA B E322 D325 N328 N331 E299 D302 N305 N308
Gene Ontology
Molecular Function
GO:0008239 dipeptidyl-peptidase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047658 alpha-amino-acid esterase activity

View graph for
Molecular Function
External links
PDB RCSB:1mpx, PDBe:1mpx, PDBj:1mpx
PDBsum1mpx
PubMed12684501
UniProtQ6YBS3

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