Structure of PDB 5cgx Chain A

Receptor sequence
>5cgxA (length=362) Species: 562 (Escherichia coli) [Search protein sequence]
GHMSGEAPLTATVDGIIQPMLKAYRIPGMAVAVLKDGKAHYFNYGVANRE
SGQRVSEQTLFEIGSVSKTLTATLGAYAAVKGGFELDDKVSQHAPWLKGS
AFDGVTMAELATYSAGGLPLQFPDEVDSNDKMQTYYRSWSPVYPAGTHRQ
FSNPSIGLFGHLAANSLGQPFEQLMSQTLLPKLGLHHTYIQVPESAMANY
AYGYSKEDKPIRATPGVLAAEAYGIKTGSADLLKFVEANMGYQGDAALKS
AIALTHTGFHSVGEMTQGLGWESYDYPVTEQVLLAGNSPAVSFQANPVTR
FAVPKAMGEQRLYNKTGSTGGFGAYVAFVPARGIAIVMLANRNYPIEARV
KAAHAILSQLAE
3D structure
PDB5cgx FOX-4 cephamycinase: an analysis of structure and function.
ChainA
Resolution1.21 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 F150 E271 K314 S317
Catalytic site (residue number reindexed from 1) S65 K68 F151 E272 K315 S318
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 1S7 A S64 K67 L119 Q120 F150 N152 Y222 F292 S317 S65 K68 L120 Q121 F151 N153 Y223 F293 S318
BS02 ZN A E5 H39 E6 H40
BS03 ZN A H1 E361 H2 E362
BS04 ZN A E124 D126 E125 D127
Gene Ontology
Molecular Function
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5cgx, PDBe:5cgx, PDBj:5cgx
PDBsum5cgx
PubMed26525784
UniProtQ9L387

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