6KM2: Carbonic anhydrase 2

Human Carbonic Anhydrase II V143I variant 15 atm CO2. Determined by X-ray diffraction at 0.9 Å resolution. Released 5 Aug 2020.

Method: X-ray diffraction
Resolution: 0.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,675
Mol. weight: 29.61 kDa
Ligands: ZN, CO2, BCT
Released: 5 Aug 2020

Explore 6KM2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6KM2 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	13-15	3
α-helix	16-19	4
α-helix	21-24	4
β-strand	32-33	2	1
β-strand	39-40	2	2
β-strand	47-50	4	2
β-strand	56-61	6	2
β-strand	66-70	5	2
β-strand	78-81	4	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	164-167	4
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

>6KM2_1 Carbonic anhydrase 2 (chains A)
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRIL
NNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHL
VHWNTKYGDFGKAVQQPDGLAILGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDP
RGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1
CO2	Carbon dioxide	C O2	2
BCT	Bicarbonate ion	C H O3	1

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

Primary citation

Structural insights into the effect of active-site mutation on the catalytic mechanism of carbonic anhydrase. Kim, J.K., Lee, C., Lim, S.W. et al. IUCrJ (2020) 7:985-994. DOI 10.1107/S2052252520011008 · 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
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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