1LUG: Full Matrix Error Analysis of Carbonic Anhydrase

Full Matrix Error Analysis of Carbonic Anhydrase. Determined by X-ray diffraction at 0.95 Å resolution. Released 9 Sept 2003.

Method: X-ray diffraction
Resolution: 0.95 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,516
Mol. weight: 30.27 kDa
Ligands: SUA, MBO, HG, ZN
Released: 9 Sept 2003

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

Secondary structure: helices and β-sheets

1LUG contains 14 α-helices and 18 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: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	16-18	3
α-helix	21-24	4
β-strand	32-33	2	1
β-strand	39-40	2	2
α-helix	44	1
β-strand	45-50	6	2
β-strand	56-61	6	2
β-strand	66-70	5	2
β-strand	78-82	5	2
β-strand	88-97	10	2
β-strand	108-109	2	1
β-strand	112	1	1
α-helix	113-114	2
β-strand	116-124	9	2
α-helix	125-127	3
α-helix	130-133	4
β-strand	140-149	10	2
α-helix	154-156	3
α-helix	157-162	6
α-helix	163-165	3
β-strand	172-174	3	2
α-helix	180-183	4
β-strand	190-195	6	2
β-strand	206-211	6	2
α-helix	214	1
β-strand	215-217	3	2
α-helix	219-225	7
β-strand	229	1	3
α-helix	232	1
β-strand	239	1	3
α-helix	245-247	3
β-strand	256-257	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carbonic Anhydrase II	A	protein	259	Homo sapiens	P00918 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1LUG_1 Carbonic Anhydrase II (chains A)
SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILN
NGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV
HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPR
GLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK

Ligands and cofactors

ID	Name	Formula	Copies
SUA	(4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester	C13 H14 N2 O3 S3	1
MBO	Mercuribenzoic acid	C7 H5 Hg O2	1
HG	Mercury (II) ion	Hg	1
ZN	Zinc ion	Zn	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Atomic resolution studies of carbonic anhydrase II. Behnke, C.A., Le Trong, I., Godden, J.W. et al. Acta Crystallogr D Biol Crystallogr (2010) 66:616-627. DOI 10.1107/S0907444910006554 · PubMed

Other PDB entries of the same protein (UniProt P00918 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3K34 0.9 Å, Human carbonic anhydrase II with a sulfonamide inhibitor
3KS3 0.9 Å, High resolution structure of Human Carbonic Anhydrase II at 0.9 A
5Y2S 0.9 Å, 7.0 atm CO2-pressurized human carbonic anhydrase II
6B00 0.9 Å, Thermostabilized mutant of human carbonic anhydrase II - A65T L100H K154N L224S L240P…
6KLZ 0.9 Å, Human Carbonic Anhydrase II V143I variant 00 atm CO2
6KM2 0.9 Å, Human Carbonic Anhydrase II V143I variant 15 atm CO2
6ROB 0.93 Å, Human Carbonic Anhydrase II in complex with 4-cyanobenzenesulfonamide
3U7C 0.93 Å, crystal structure of the V143I mutant of human carbonic anhydrase II
6KM0 0.93 Å, Human Carbonic Anhydrase II V143I variant 07 atm CO2
6ROE 0.94 Å, Human Carbonic Anhydrase II in complex with fluorinated benzenesulfonamide
6SBL 0.94 Å, Human Carbonic Anhydrase II in complex with 4-hexylbenzenesulfonamide
6RH4 0.95 Å, Human Carbonic Anhydrase II in complex with 4-Nitrobenzenesulfonamide.

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