4QJO

Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with inhibitor

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	7
Details	BINDING SITE FOR RESIDUE EDO A 301

Chain	Residue
A	ALA188
A	SER260
A	PHE261
A	HOH426
A	HOH548
C	PRO9
D	LEU25

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	HIS117
A	V1F303
A	HIS91
A	HIS93

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE V1F A 303

Chain	Residue
A	ASN64
A	GLN89
A	HIS91
A	HIS93
A	GLU104
A	HIS117
A	ALA129
A	VAL141
A	LEU197
A	THR198
A	THR199
A	PRO200
A	ZN302

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 301

Chain	Residue
B	ASP156
B	SER160
B	GLN221
B	HOH575

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 302

Chain	Residue
B	ASN152
B	SER154
B	GLU181

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 303

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	V1F304

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE V1F B 304

Chain	Residue
B	ASN64
B	GLN89
B	HIS91
B	HIS93
B	HIS117
B	VAL119
B	ALA129
B	SER133
B	LEU197
B	THR198
B	THR199
B	PRO200
B	PRO201
B	TRP208
B	ZN303

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	V1F302

---

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE V1F C 302

Chain	Residue
C	ASN64
C	GLN89
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	ALA129
C	SER130
C	SER133
C	LEU197
C	THR198
C	THR199
C	PRO201
C	TRP208
C	ZN301
C	HOH529
C	HOH578

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	V1F302

---

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE V1F D 302

Chain	Residue
D	ASN64
D	GLN89
D	HIS91
D	HIS93
D	HIS117
D	VAL119
D	SER133
D	LEU197
D	THR198
D	THR199
D	PRO200
D	TRP208
D	ZN301
D	HOH526
D	HOH540

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER103-VAL119

---

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":"11493685","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	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---