6QUT

Three dimensional structure of human carbonic anhydrase IX in complex with benzenesulfonamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0008270	molecular_function	zinc ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0008270	molecular_function	zinc ion binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0008270	molecular_function	zinc ion binding
D	0004089	molecular_function	carbonate dehydratase activity
D	0008270	molecular_function	zinc 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	HIS94
A	HIS96
A	HIS119
A	J8N302

---

site_id	AC2
Number of Residues	14
Details	binding site for residue J8N A 302

Chain	Residue
A	HIS96
A	HIS119
A	VAL131
A	VAL143
A	LEU198
A	THR199
A	THR200
A	TRP209
A	ZN301
A	ASN62
A	SER65
A	GLN67
A	GLN92
A	HIS94

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS94
B	HIS96
B	HIS119
B	J8N302

---

site_id	AC4
Number of Residues	15
Details	binding site for residue J8N B 302

Chain	Residue
B	ASN62
B	SER65
B	GLN67
B	GLN92
B	HIS94
B	HIS96
B	HIS119
B	VAL131
B	VAL143
B	LEU198
B	THR199
B	THR200
B	TRP209
B	ZN301
B	HOH483

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS94
C	HIS96
C	HIS119
C	J8N302

---

site_id	AC6
Number of Residues	16
Details	binding site for residue J8N C 302

Chain	Residue
C	ASN62
C	SER65
C	GLN67
C	GLN92
C	HIS94
C	HIS96
C	HIS119
C	VAL143
C	LEU198
C	THR199
C	THR200
C	PRO201
C	TRP209
C	ZN301
C	J8N303
C	HOH479

---

site_id	AC7
Number of Residues	10
Details	binding site for residue J8N C 303

Chain	Residue
C	GLN67
C	LEU91
C	GLN92
C	ARG130
C	VAL131
C	J8N302
C	HOH615
D	ARG130
D	ASP132
D	J8N303

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS94
D	HIS96
D	HIS119
D	J8N302

---

site_id	AC9
Number of Residues	16
Details	binding site for residue J8N D 302

Chain	Residue
D	ASN62
D	SER65
D	GLN67
D	GLN92
D	HIS94
D	HIS96
D	HIS119
D	VAL143
D	LEU198
D	THR199
D	THR200
D	PRO201
D	TRP209
D	ZN301
D	J8N303
D	HOH415

---

site_id	AD1
Number of Residues	10
Details	binding site for residue J8N D 303

Chain	Residue
C	ARG130
C	J8N303
C	HOH541
D	GLN67
D	LEU91
D	GLN92
D	ARG130
D	VAL131
D	J8N302
D	HOH471

---

Functional Information from PROSITE/UniProt

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

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":"19805286","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	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18703501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---