1G6A: Pse-4 carbenicillinase, R234K mutant

Pse-4 carbenicillinase, R234K mutant. Determined by X-ray diffraction at 1.75 Å resolution. Released 21 Feb 2001.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Pseudomonas aeruginosa
Chains: 1
Atoms: 2,312
Mol. weight: 29.62 kDa
Released: 21 Feb 2001

Explore 1G6A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G6A contains 15 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 15 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	27-39	13
β-strand	43-50	8	1
β-strand	55-60	5	1
β-strand	66-67	2	2
α-helix	69-72	4
α-helix	73-85	13
β-strand	94-96	3	3
α-helix	99-101	3
α-helix	109-111	3
β-strand	116-118	3	3
α-helix	119-129	11
α-helix	132-141	10
α-helix	144-154	11
β-strand	161	1	2
α-helix	168-170	3
β-strand	180-181	2	2
α-helix	183-195	13
α-helix	201-212	12
α-helix	221-224	4
α-helix	225-226	2
β-strand	230-237	8	1
α-helix	240-242	3
β-strand	244-252	9	1
β-strand	256-266	11	1
α-helix	272-291	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Beta-lactamase pse-4	A	protein	271	Pseudomonas aeruginosa	P16897 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1G6A_1 BETA-LACTAMASE PSE-4 (chains A)
SSSKFQQVEQDVKAIEVSLSARIGVSVLDTQNGEYWDYNGNQRFPLTSTFKTIACAKLLY
DAEQGKVNPNSTVEIKKADLVTYSPVIEKQVGQAITLDDACFATMTTSDNTAANIILSAV
GGPKGVTDFLRQIGDKETRLDRIEPDLNEGKLGDLRDTTTPKAIASTLNKFLFGSALSEM
NQKKLESWMVNNQVTGNLLRSVLPAGWNIADKSGAGGFGARSITAVVWSEHQAPIIVSIY
LAQTQASMEERNDAIVKIGHSIFDVYTSQSR

Primary citation

Insights into the molecular basis for the carbenicillinase activity of PSE-4 beta-lactamase from crystallographic and kinetic studies. Lim, D., Sanschagrin, F., Passmore, L. et al. Biochemistry (2001) 40:395-402. DOI 10.1021/bi001653v · PubMed

Other PDB entries of the same protein (UniProt P16897 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ID4 1.05 Å, Crystal structure of chimeric beta-lactamase cTEM-17m
4R4S 1.1 Å, Crystal structure of chimeric beta-lactamase cTEM-19m at 1.1 angstrom resolution
4QY6 1.15 Å, Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations
4R4R 1.2 Å, Crystal structure of chimeric beta-lactamase cTEM-19m at 1.2 angstrom resolution
4QY5 1.5 Å, Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations
1G68 1.95 Å, Pse-4 carbenicillinase, wild type
8J6Y 2.4 Å, Crystal structure of class A beta-lactamase PSE-4 WT- Apo state

Browse structure collections

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