Structure of PDB 1o07 Chain B

Receptor sequence
>1o07B (length=358) Species: 562 (Escherichia coli) [Search protein sequence]
APQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQP
VTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNG
ITLLHLATYTAGGLPLLVPDEVKSSSDLLRFYQNWQPAWAPGTQRLEANS
SIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGY
REGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQ
LAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITP
PTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAA
WQILNALQ
3D structure
PDB1o07 Structural Aspects for Evolution of beta-Lactamases from Penicillin-Binding Proteins
ChainB
Resolution1.71 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S64 K67 Y112 A114 V121 E150 A151 G156 E272 K315 A318
Catalytic site (residue number reindexed from 1) S61 K64 Y109 A111 V118 E147 A148 G153 E269 K312 A315
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 MXG B G63 S64 S212 Y221 L293 A318 T319 N343 G60 S61 S209 Y218 L290 A315 T316 N340
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1o07, PDBe:1o07, PDBj:1o07
PDBsum1o07
PubMed12904027
UniProtP00811|AMPC_ECOLI Beta-lactamase (Gene Name=ampC)

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