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Three dimensional structure of human carbonic anhydrase IX

Analyse Three dimensional structure of human carbonic anhydrase IX in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FE2
Type: protein
Length: 997 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase 9
EC: 4.2.1.1
UniProt: Q16790
Ligands: ZN
Pockets: 11 · best druggability 0.88

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, D	Carbonic anhydrase 9 (EC 4.2.1.1)	protein	251	16% helix, 34% strand	Q16790
B	Carbonic anhydrase 9 (EC 4.2.1.1)	protein	244	15% helix, 35% strand	Q16790

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	829	0.88	0.91	94	empty
2	429	0.70	0.81	44	empty
3	353	0.69	0.82	46	empty
4	86	0.61	0.89	32	empty
5	78	0.56	0.87	22	empty

Interfaces

5 interfaces between chains.

A–B · 874 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 539 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 517 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 436 Å² buried · 9 hydrogen bonds · protein-protein
A–D · 260 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6FE2 · Three dimensional structure of human carbonic anhydrase IX · the same entry in another collection · chain D against D, TM-score 1.00
Q16790 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 9 (Q16790) · a predicted model of the same protein · chain B against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q16790
Elsewhere: RCSB PDB 6FE2 · PDBe 6FE2 · UniProt Q16790

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