4QJW

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	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS91
A	HIS93
A	HIS117
A	WWO302

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE WWO A 302

Chain	Residue
A	GLU104
A	HIS117
A	ALA129
A	SER130
A	SER133
A	LEU197
A	THR198
A	THR199
A	PRO200
A	ZN301
A	HOH672
A	ASN64
A	SER67
A	GLN89
A	HIS91
A	HIS93

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	SER42
A	LEU43
A	THR44
A	GLY80
A	TYR190
A	ARG192

---

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

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	WWO302

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE WWO B 302

Chain	Residue
B	ASN64
B	GLN89
B	HIS91
B	HIS93
B	GLU104
B	HIS117
B	VAL119
B	ALA129
B	LEU197
B	THR198
B	THR199
B	ZN301
B	HOH604

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 303

Chain	Residue
B	ASN71
B	LEU72
B	THR88
B	HOH428
B	HOH480
B	HOH521

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 304

Chain	Residue
B	ASP156
B	SER160
B	GLN221
B	HOH645

---

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

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	WWO302

---

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE WWO C 302

Chain	Residue
C	ASN64
C	GLN89
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	ALA129
C	SER133
C	LEU197
C	THR198
C	THR199
C	PRO200
C	ZN301
C	HOH556
C	HOH610

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
C	ASP156
C	SER160
C	HOH615

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	WWO302

---

site_id	BC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE WWO D 302

Chain	Residue
D	ASN64
D	GLN89
D	HIS91
D	HIS93
D	GLU104
D	HIS117
D	VAL119
D	ALA129
D	SER133
D	LEU197
D	THR198
D	THR199
D	PRO200
D	ZN301
D	HOH614
D	HOH628
D	HOH722

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 303

Chain	Residue
D	HOH546
D	HOH699
D	ASP156
D	SER160
D	GLN221

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 304

Chain	Residue
D	LEU43
D	ARG192
D	HOH650

---

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 305

Chain	Residue
D	GLN163
D	HOH547
D	HOH646

---

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

---