Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5JN8

Crystal Structure for the complex of human carbonic anhydrase IV and acetazolamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005515	molecular_function	protein binding
A	0005791	cellular_component	rough endoplasmic reticulum
A	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
A	0005794	cellular_component	Golgi apparatus
A	0005802	cellular_component	trans-Golgi network
A	0005886	cellular_component	plasma membrane
A	0008270	molecular_function	zinc ion binding
A	0009897	cellular_component	external side of plasma membrane
A	0009986	cellular_component	cell surface
A	0015701	biological_process	bicarbonate transport
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0016324	cellular_component	apical plasma membrane
A	0016829	molecular_function	lyase activity
A	0030658	cellular_component	transport vesicle membrane
A	0030667	cellular_component	secretory granule membrane
A	0031526	cellular_component	brush border membrane
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0070062	cellular_component	extracellular exosome
A	0098552	cellular_component	side of membrane
B	0004089	molecular_function	carbonate dehydratase activity
B	0005515	molecular_function	protein binding
B	0005791	cellular_component	rough endoplasmic reticulum
B	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
B	0005794	cellular_component	Golgi apparatus
B	0005802	cellular_component	trans-Golgi network
B	0005886	cellular_component	plasma membrane
B	0008270	molecular_function	zinc ion binding
B	0009897	cellular_component	external side of plasma membrane
B	0009986	cellular_component	cell surface
B	0015701	biological_process	bicarbonate transport
B	0016020	cellular_component	membrane
B	0016323	cellular_component	basolateral plasma membrane
B	0016324	cellular_component	apical plasma membrane
B	0016829	molecular_function	lyase activity
B	0030658	cellular_component	transport vesicle membrane
B	0030667	cellular_component	secretory granule membrane
B	0031526	cellular_component	brush border membrane
B	0046872	molecular_function	metal ion binding
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0070062	cellular_component	extracellular exosome
B	0098552	cellular_component	side of membrane
C	0004089	molecular_function	carbonate dehydratase activity
C	0005515	molecular_function	protein binding
C	0005791	cellular_component	rough endoplasmic reticulum
C	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
C	0005794	cellular_component	Golgi apparatus
C	0005802	cellular_component	trans-Golgi network
C	0005886	cellular_component	plasma membrane
C	0008270	molecular_function	zinc ion binding
C	0009897	cellular_component	external side of plasma membrane
C	0009986	cellular_component	cell surface
C	0015701	biological_process	bicarbonate transport
C	0016020	cellular_component	membrane
C	0016323	cellular_component	basolateral plasma membrane
C	0016324	cellular_component	apical plasma membrane
C	0016829	molecular_function	lyase activity
C	0030658	cellular_component	transport vesicle membrane
C	0030667	cellular_component	secretory granule membrane
C	0031526	cellular_component	brush border membrane
C	0046872	molecular_function	metal ion binding
C	0048471	cellular_component	perinuclear region of cytoplasm
C	0070062	cellular_component	extracellular exosome
C	0098552	cellular_component	side of membrane
D	0004089	molecular_function	carbonate dehydratase activity
D	0005515	molecular_function	protein binding
D	0005791	cellular_component	rough endoplasmic reticulum
D	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
D	0005794	cellular_component	Golgi apparatus
D	0005802	cellular_component	trans-Golgi network
D	0005886	cellular_component	plasma membrane
D	0008270	molecular_function	zinc ion binding
D	0009897	cellular_component	external side of plasma membrane
D	0009986	cellular_component	cell surface
D	0015701	biological_process	bicarbonate transport
D	0016020	cellular_component	membrane
D	0016323	cellular_component	basolateral plasma membrane
D	0016324	cellular_component	apical plasma membrane
D	0016829	molecular_function	lyase activity
D	0030658	cellular_component	transport vesicle membrane
D	0030667	cellular_component	secretory granule membrane
D	0031526	cellular_component	brush border membrane
D	0046872	molecular_function	metal ion binding
D	0048471	cellular_component	perinuclear region of cytoplasm
D	0070062	cellular_component	extracellular exosome
D	0098552	cellular_component	side of membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue AZM A 701

Chain	Residue
A	GLN92
A	SO4705
A	HIS94
A	HIS96
A	HIS119
A	LEU198
A	THR199
A	THR200
A	TRP209
A	ZN702

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 702

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	AZM701

site_id	AC3
Number of Residues	7
Details	binding site for residue SO4 A 703

Chain	Residue
A	ARG27
A	LEU195
A	ARG254
A	THR255
A	ACT708
A	HOH834
A	HOH884

site_id	AC4
Number of Residues	6
Details	binding site for residue SO4 A 704

Chain	Residue
A	GLY50
A	TYR51
A	ASP52
A	LYS53
A	HOH838
A	HOH898

site_id	AC5
Number of Residues	5
Details	binding site for residue SO4 A 705

Chain	Residue
A	ASN62
A	HIS64
A	GLN92
A	HIS94
A	AZM701

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 A 706

Chain	Residue
A	ARG46
A	GLU187
C	ASN72
C	LYS91

site_id	AC7
Number of Residues	9
Details	binding site for residue ACT A 707

Chain	Residue
A	SER98
A	ASP99
A	LEU100
A	PRO101
A	ALA115
A	ALA150
A	ILE223
A	LEU224
A	HOH861

site_id	AC8
Number of Residues	2
Details	binding site for residue ACT A 708

Chain	Residue
A	THR255
A	SO4703

site_id	AC9
Number of Residues	7
Details	binding site for residue GOL A 709

Chain	Residue
A	PHE48
A	SER50
A	SER78
A	ILE79
A	SER80
A	PRO87
C	GLN60

site_id	AD1
Number of Residues	12
Details	binding site for residue AZM B 701

Chain	Residue
B	GLN92
B	HIS94
B	HIS96
B	HIS119
B	LEU198
B	THR199
B	THR200
B	ZN702
B	SO4706
B	HOH802
B	HOH842
B	HOH876

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN B 702

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	AZM701

site_id	AD3
Number of Residues	7
Details	binding site for residue SO4 B 703

Chain	Residue
B	ARG27
B	LEU195
B	ARG254
B	THR255
B	HOH806
B	HOH845
B	HOH886

site_id	AD4
Number of Residues	7
Details	binding site for residue SO4 B 704

Chain	Residue
B	GLY50
B	TYR51
B	ASP52
B	LYS53
B	HOH803
B	HOH907
B	HOH944

site_id	AD5
Number of Residues	4
Details	binding site for residue SO4 B 705

Chain	Residue
B	LYS233
C	GLY45
C	ARG46
C	ARG189

site_id	AD6
Number of Residues	4
Details	binding site for residue SO4 B 706

Chain	Residue
B	ASN62
B	HIS94
B	AZM701
B	HOH864

site_id	AD7
Number of Residues	5
Details	binding site for residue ACT B 707

Chain	Residue
B	LYS15
D	GLU155
D	GLN158
D	GLU162
D	HOH802

site_id	AD8
Number of Residues	8
Details	binding site for residue GOL B 708

Chain	Residue
B	ILE79
B	SER80
B	PRO87
B	HOH859
D	GLN60
D	MET67
B	PHE48
B	SER78

site_id	AD9
Number of Residues	5
Details	binding site for residue GOL B 709

Chain	Residue
B	ARG193
B	TYR194
B	THR255
B	HOH884
B	HOH886

site_id	AE1
Number of Residues	9
Details	binding site for residue AZM C 701

Chain	Residue
C	GLN92
C	HIS94
C	HIS96
C	HIS119
C	LEU198
C	THR199
C	THR200
C	TRP209
C	ZN702

site_id	AE2
Number of Residues	4
Details	binding site for residue ZN C 702

Chain	Residue
C	HIS94
C	HIS96
C	HIS119
C	AZM701

site_id	AE3
Number of Residues	6
Details	binding site for residue SO4 C 703

Chain	Residue
C	ARG27
C	LEU195
C	ARG254
C	THR255
C	HOH838
C	HOH839

site_id	AE4
Number of Residues	7
Details	binding site for residue SO4 C 704

Chain	Residue
C	GLY50
C	TYR51
C	ASP52
C	LYS53
C	HOH808
C	HOH927
C	HOH941

site_id	AE5
Number of Residues	4
Details	binding site for residue ACT C 705

Chain	Residue
A	ARG46
A	ARG189
C	ASN72
C	GLN89

site_id	AE6
Number of Residues	8
Details	binding site for residue GOL C 706

Chain	Residue
C	LYS103
C	ASP243
C	VAL245
C	PRO247
C	HOH818
C	HOH905
C	HOH937
C	HOH955

site_id	AE7
Number of Residues	4
Details	binding site for residue GOL C 707

Chain	Residue
C	SER50
C	ASN72
C	SER78
C	GLN89

site_id	AE8
Number of Residues	13
Details	binding site for residue AZM D 701

Chain	Residue
D	GLN92
D	HIS94
D	HIS96
D	HIS119
D	VAL121
D	LEU198
D	THR199
D	THR200
D	TRP209
D	ZN702
D	HOH842
D	HOH871
D	HOH1016

site_id	AE9
Number of Residues	4
Details	binding site for residue ZN D 702

Chain	Residue
D	HIS94
D	HIS96
D	HIS119
D	AZM701

site_id	AF1
Number of Residues	5
Details	binding site for residue SO4 D 703

Chain	Residue
D	ARG27
D	ARG254
D	THR255
D	HOH835
D	HOH853

site_id	AF2
Number of Residues	5
Details	binding site for residue SO4 D 704

Chain	Residue
A	GLU2
D	GLY50
D	TYR51
D	ASP52
D	LYS53

site_id	AF3
Number of Residues	8
Details	binding site for residue ACT D 705

Chain	Residue
D	ASP99
D	LEU100
D	PRO101
D	ALA115
D	ALA150
D	ILE223
D	LEU224
D	HOH815

Functional Information from PROSITE/UniProt

site_id	PS00162
Number of Residues	17
Details	ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHsLdgehFamEMHIV

Chain	Residue	Details
A	SER105-VAL121

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8942978","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Lipidation: {"description":"GPI-anchor amidated serine","evidences":[{"source":"PubMed","id":"7625839","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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