1ALI: Alkaline phosphatase mutant

Alkaline phosphatase mutant (H412N). Determined by X-ray diffraction at 2.2 Å resolution. Released 14 Nov 1995.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Escherichia coli
Chains: 2
Atoms: 6,813
Mol. weight: 94.64 kDa
Ligands: PO4, MG, ZN
Released: 14 Nov 1995

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

Secondary structure: helices and β-sheets

1ALI contains 51 α-helices and 59 β-strands across 2 chains. 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: 25 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	30-34	5
α-helix	41-42	2
β-strand	44-50	7	1
α-helix	55-66	12
β-strand	80-85	6	1
β-strand	88-89	2	2
β-strand	96-97	2	2
α-helix	102-111	10
β-strand	116	1	2
β-strand	120	1	3
β-strand	122	1	4
β-strand	128	1	4
α-helix	132-138	7
β-strand	142-150	9	1
α-helix	154-157	4
β-strand	163	1	3
α-helix	171-177	7
α-helix	179-181	3
α-helix	183-185	3
α-helix	191-198	8
β-strand	202-206	5	1
α-helix	209-212	4
β-strand	214	1	5
β-strand	215	1	6
β-strand	221	1	6
β-strand	224	1	5
α-helix	225-231	7
β-strand	235-237	3	1
α-helix	240-245	6
β-strand	255-258	4	1
α-helix	264-266	3
β-strand	268-269	2	7
α-helix	271-273	3
β-strand	274-275	2	8
α-helix	277-280	4
α-helix	282-283	2
β-strand	284	1	8
β-strand	287-288	2	7
α-helix	290-292	3
α-helix	297-298	2
α-helix	299-311	13
β-strand	317-323	7	1
α-helix	325-331	7
α-helix	335-359	25
β-strand	362-368	7	1
β-strand	371	1	9
β-strand	375-377	3	8
β-strand	386-391	6	8
β-strand	397-402	6	8
α-helix	410-412	3
β-strand	413	1	9
β-strand	417-422	6	1
α-helix	426-429	4
β-strand	431-434	4	1
α-helix	435-445	11

Chain B: 26 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	30-34	5
α-helix	41-42	2
β-strand	44-50	7	10
α-helix	55-66	12
α-helix	75-77	3
β-strand	80-85	6	10
β-strand	88-89	2	11
β-strand	96-97	2	11
α-helix	102-111	10
β-strand	120	1	12
β-strand	122	1	13
β-strand	128	1	13
α-helix	132-138	7
β-strand	142-150	9	10
α-helix	154-157	4
β-strand	163	1	12
α-helix	171-177	7
α-helix	179-181	3
α-helix	183-185	3
α-helix	191-198	8
β-strand	202-206	5	10
α-helix	209-212	4
β-strand	214	1	14
β-strand	215	1	15
β-strand	221	1	15
β-strand	224	1	14
α-helix	225-231	7
α-helix	234	1
β-strand	235-237	3	10
α-helix	240-245	6
β-strand	255-258	4	10
α-helix	264-266	3
β-strand	268-269	2	16
α-helix	271-273	3
β-strand	274-275	2	17
α-helix	277-280	4
α-helix	282-283	2
β-strand	284	1	17
β-strand	287-288	2	16
α-helix	290-292	3
α-helix	299-310	12
β-strand	317-323	7	10
α-helix	325-331	7
α-helix	335-359	25
β-strand	362-368	7	10
β-strand	371	1	18
β-strand	375-377	3	17
β-strand	386-391	6	17
β-strand	397-402	6	17
α-helix	410-412	3
β-strand	413	1	18
β-strand	417-422	6	10
α-helix	426-429	4
β-strand	431-434	4	10
α-helix	435-445	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alkaline phosphatase	A, B	protein	449	Escherichia coli	P00634 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1ALI_1 ALKALINE PHOSPHATASE (chains A, B)
TPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITA
ARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGAL
GVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPG
NALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDA
ASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLA
QMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEG
NTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQENTGSQLRIA
AYGPHAANVVGLTDQTDLFYTMKAALGLK

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2
MG	Magnesium ion	Mg	2
ZN	Zinc ion	Zn	4

Primary citation

Escherichia coli alkaline phosphatase: X-ray structural studies of a mutant enzyme (His-412-->Asn) at one of the catalytically important zinc binding sites. Ma, L., Tibbitts, T.T., Kantrowitz, E.R. Protein Sci (1995) 4:1498-1506. PubMed

Other PDB entries of the same protein (UniProt P00634 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3TG0 1.2 Å, E. coli alkaline phosphatase with bound inorganic phosphate
3BDF 1.4 Å, Crystal structure of metal-free E. coli alkaline phosphatase (T155V)
3BDG 1.4 Å, Crystal structure of wild-type/T155V mixed dimer of E. coli alkaline phosphatase
1Y6V 1.6 Å, Structure of E. coli Alkaline Phosphatase in presence of cobalt at 1.60 A resolution
1ED8 1.75 Å, Structure of E. Coli alkaline phosphatase inhibited by the inorganic phosphate at 1.75A…
1ED9 1.75 Å, Structure of E. Coli alkaline phosphatase without the inorganic phosphate at 1.75A…
1Y7A 1.77 Å, Structure of D153H/K328W E. coli alkaline phosphatase in presence of cobalt at 1.77 A…
7N6M 1.82 Å, Crystal structure of the substrate-binding domain of E. coli DnaK in complex with the…
3BDH 1.85 Å, Crystal structure of zinc-deficient wild-type E. coli alkaline phosphatase
1B8J 1.9 Å, Alkaline phosphatase complexed with vanadate
1ALK 2.0 Å, Reaction mechanism of alkaline phosphatase based on crystal structures. Two metal ion…
1EW9 2.0 Å, Alkaline phosphatase (e.c. 3.1.3.1) complex with mercaptomethyl phosphonate

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