5LLO

Crystal structure of human carbonic anhydrase isozyme XII with 3-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-2,5,6-trifluoro-4-[(2-hy-droxyethyl)sulfonyl]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	HIS91
A	HIS93
A	HIS117
A	5EF303

---

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 302

Chain	Residue
A	ASP156
A	SER160
A	HOH462

---

site_id	AC3
Number of Residues	14
Details	binding site for residue 5EF A 303

Chain	Residue
A	HIS91
A	HIS93
A	GLU104
A	HIS117
A	VAL119
A	SER130
A	LEU197
A	THR198
A	THR199
A	PRO200
A	ZN301
A	HOH546
A	ASN64
A	SER67

---

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

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	5EF303

---

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

Chain	Residue
B	THR44
B	LEU46
B	GLY80
B	LEU81
B	TYR190
B	ARG192

---

site_id	AC6
Number of Residues	14
Details	binding site for residue 5EF B 303

Chain	Residue
B	ASN64
B	SER67
B	HIS91
B	HIS93
B	HIS117
B	VAL119
B	ALA129
B	SER133
B	LEU197
B	THR198
B	THR199
B	ZN301
B	HOH402
B	HOH598

---

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

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	5EF302

---

site_id	AC8
Number of Residues	16
Details	binding site for residue 5EF C 302

Chain	Residue
C	ASN64
C	GLN89
C	HIS91
C	HIS93
C	GLU104
C	HIS117
C	VAL119
C	ALA129
C	SER130
C	LEU197
C	THR198
C	THR199
C	PRO200
C	ZN301
C	HOH518
C	HOH552

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	5EF303

---

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO D 302

Chain	Residue
D	SER42
D	THR44
D	LEU46
D	GLY80
D	TYR190
D	ARG192

---

site_id	AD2
Number of Residues	13
Details	binding site for residue 5EF D 303

Chain	Residue
D	ASN64
D	HIS91
D	HIS93
D	GLU104
D	HIS117
D	VAL119
D	ALA129
D	SER130
D	LEU197
D	THR198
D	THR199
D	ZN301
D	HOH403

---

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

---