3K34: Carbonic anhydrase 2

Human carbonic anhydrase II with a sulfonamide inhibitor. Determined by X-ray diffraction at 0.9 Å resolution. Released 12 May 2010.

Method: X-ray diffraction
Resolution: 0.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,387
Mol. weight: 30.31 kDa
Ligands: HGB, ZN, SUA
Released: 12 May 2010

Explore 3K34 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3K34 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	125-128	3
α-helix	131-134	4
β-strand	141-150	10	2
α-helix	155-157	3
α-helix	158-163	6
α-helix	164-166	3
β-strand	173-175	3	2
α-helix	181-184	4
β-strand	191-196	6	2
β-strand	207-212	6	2
α-helix	215	1
β-strand	216-218	3	2
α-helix	220-226	7
β-strand	230	1	3
α-helix	233	1
β-strand	240	1	3
α-helix	246-248	3
β-strand	257-258	2	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carbonic anhydrase 2	A	protein	260	Homo sapiens	P00918 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3K34_1 Carbonic anhydrase 2 (chains A)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRIL
NNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHL
VHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDP
RGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK

Ligands and cofactors

ID	Name	Formula	Copies
HGB	4-(hydroxymercury)benzoic acid	C7 H6 Hg O3	1
ZN	Zinc ion	Zn	1
SUA	(4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester	C13 H14 N2 O3 S3	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:

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.
1LUG 0.95 Å, Full Matrix Error Analysis of Carbonic Anhydrase

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