Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5TUO

Crystal structure of the complex of Helicobacter pylori alpha-carbonic anhydrase with 5-amino-1,3,4-thiadiazole-2-sulfonamide inhibitor.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0006885	biological_process	regulation of pH
A	0008270	molecular_function	zinc ion binding
A	0015670	biological_process	carbon dioxide transport
A	0046872	molecular_function	metal ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0006885	biological_process	regulation of pH
B	0008270	molecular_function	zinc ion binding
B	0015670	biological_process	carbon dioxide transport
B	0046872	molecular_function	metal ion binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0006885	biological_process	regulation of pH
C	0008270	molecular_function	zinc ion binding
C	0015670	biological_process	carbon dioxide transport
C	0046872	molecular_function	metal ion binding
D	0004089	molecular_function	carbonate dehydratase activity
D	0006885	biological_process	regulation of pH
D	0008270	molecular_function	zinc ion binding
D	0015670	biological_process	carbon dioxide transport
D	0046872	molecular_function	metal ion binding
E	0004089	molecular_function	carbonate dehydratase activity
E	0006885	biological_process	regulation of pH
E	0008270	molecular_function	zinc ion binding
E	0015670	biological_process	carbon dioxide transport
E	0046872	molecular_function	metal ion binding
F	0004089	molecular_function	carbonate dehydratase activity
F	0006885	biological_process	regulation of pH
F	0008270	molecular_function	zinc ion binding
F	0015670	biological_process	carbon dioxide transport
F	0046872	molecular_function	metal ion binding
G	0004089	molecular_function	carbonate dehydratase activity
G	0006885	biological_process	regulation of pH
G	0008270	molecular_function	zinc ion binding
G	0015670	biological_process	carbon dioxide transport
G	0046872	molecular_function	metal ion binding
H	0004089	molecular_function	carbonate dehydratase activity
H	0006885	biological_process	regulation of pH
H	0008270	molecular_function	zinc ion binding
H	0015670	biological_process	carbon dioxide transport
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS110
A	HIS112
A	HIS129
A	1SA303

site_id	AC2
Number of Residues	5
Details	binding site for residue CL A 302

Chain	Residue
A	MET115
A	GLU116
A	PHE117
A	SER127
A	HIS129

site_id	AC3
Number of Residues	9
Details	binding site for residue 1SA A 303

Chain	Residue
A	HIS84
A	THR86
A	HIS110
A	HIS112
A	HIS129
A	LEU190
A	THR191
A	ALA192
A	ZN301

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS110
B	HIS112
B	HIS129
B	1SA303

site_id	AC5
Number of Residues	6
Details	binding site for residue CL B 302

Chain	Residue
B	MET115
B	GLU116
B	PHE117
B	SER127
B	HIS129
B	ALA143

site_id	AC6
Number of Residues	8
Details	binding site for residue 1SA B 303

Chain	Residue
B	HIS110
B	HIS112
B	HIS129
B	VAL131
B	LEU190
B	THR191
B	ALA192
B	ZN301

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS110
C	HIS112
C	HIS129
C	1SA303

site_id	AC8
Number of Residues	6
Details	binding site for residue CL C 302

Chain	Residue
C	MET115
C	GLU116
C	PHE117
C	SER127
C	HIS129
C	ALA143

site_id	AC9
Number of Residues	10
Details	binding site for residue 1SA C 303

Chain	Residue
C	THR83
C	HIS84
C	THR86
C	HIS110
C	HIS112
C	HIS129
C	LEU190
C	THR191
C	ALA192
C	ZN301

site_id	AD1
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS110
D	HIS112
D	HIS129
D	1SA303

site_id	AD2
Number of Residues	5
Details	binding site for residue CL D 302

Chain	Residue
D	MET115
D	GLU116
D	PHE117
D	SER127
D	HIS129

site_id	AD3
Number of Residues	9
Details	binding site for residue 1SA D 303

Chain	Residue
D	TRP23
D	THR83
D	HIS84
D	HIS110
D	HIS112
D	LEU190
D	THR191
D	ALA192
D	ZN301

site_id	AD4
Number of Residues	4
Details	binding site for residue ZN E 301

Chain	Residue
E	HIS110
E	HIS112
E	HIS129
E	1SA303

site_id	AD5
Number of Residues	5
Details	binding site for residue CL E 302

Chain	Residue
E	MET115
E	GLU116
E	PHE117
E	SER127
E	HIS129

site_id	AD6
Number of Residues	9
Details	binding site for residue 1SA E 303

Chain	Residue
E	HIS110
E	HIS112
E	HIS129
E	VAL131
E	LEU190
E	THR191
E	ALA192
E	TRP201
E	ZN301

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN F 301

Chain	Residue
F	HIS110
F	HIS112
F	HIS129
F	1SA302

site_id	AD8
Number of Residues	7
Details	binding site for residue 1SA F 302

Chain	Residue
F	LEU190
F	THR191
F	ALA192
F	ZN301
F	HIS110
F	HIS112
F	HIS129

site_id	AD9
Number of Residues	4
Details	binding site for residue ZN G 301

Chain	Residue
G	HIS110
G	HIS112
G	HIS129
G	1SA303

site_id	AE1
Number of Residues	5
Details	binding site for residue CL G 302

Chain	Residue
G	MET115
G	GLU116
G	PHE117
G	SER127
G	HIS129

site_id	AE2
Number of Residues	6
Details	binding site for residue 1SA G 303

Chain	Residue
G	HIS110
G	HIS112
G	HIS129
G	LEU190
G	THR191
G	ZN301

site_id	AE3
Number of Residues	4
Details	binding site for residue ZN H 301

Chain	Residue
H	HIS110
H	HIS112
H	HIS129
H	1SA303

site_id	AE4
Number of Residues	4
Details	binding site for residue CL H 302

Chain	Residue
H	GLU116
H	PHE117
H	SER127
H	HIS129

site_id	AE5
Number of Residues	9
Details	binding site for residue 1SA H 303

Chain	Residue
H	TRP23
H	HIS84
H	THR86
H	HIS110
H	HIS112
H	LEU190
H	THR191
H	ALA192
H	ZN301

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)