Structure of PDB 1ong Chain A

Receptor sequence
>1ongA (length=265) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
SPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVV
LCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAA
AITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPG
DARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVL
PAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQ
QIAGIGAALIEHWQR
3D structure
PDB1ong Inhibition of Class A and Class C Beta-Lactamases by Penems: Crystallographic Structures of a Novel 1,4-Thiazepine Intermediate
ChainA
Resolution1.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S70 K73 S130 E166 K234 A237
Catalytic site (residue number reindexed from 1) S45 K48 S105 E141 K209 A212
Enzyme Commision number 3.5.2.6: beta-lactamase.
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 MA4 A V224 P226 V261 I263 I279 A280 A284 V199 P201 V234 I236 I252 A253 A257
BS02 MA4 A L220 I279 L195 I252
BS03 WY4 A S70 Y105 S130 N132 N170 G236 A237 S45 Y80 S105 N107 N145 G211 A212 PDBbind-CN: -logKd/Ki=8.05,IC50=9nM
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:1ong, PDBe:1ong, PDBj:1ong
PDBsum1ong
PubMed14609325
UniProtP0AD64|BLA1_KLEPN Beta-lactamase SHV-1 (Gene Name=bla)

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