4QJ0

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	WWX303

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
A	ASP156
A	SER160
A	HOH465

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE WWX A 303

Chain	Residue
A	SER67
A	THR88
A	GLN89
A	HIS91
A	HIS93
A	HIS117
A	VAL119
A	LEU139
A	VAL141
A	LEU197
A	THR198
A	THR199
A	PRO200
A	PRO201
A	ZN301
A	HOH499
A	HOH609
A	TRP4
A	ASN64

---

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

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	WWX303

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 302

Chain	Residue
B	SER42
B	THR44
B	LEU46
B	GLY80
B	LEU81
B	TYR190
B	ARG192

---

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE WWX B 303

Chain	Residue
B	TRP4
B	ASN64
B	THR88
B	GLN89
B	HIS91
B	HIS93
B	HIS117
B	VAL119
B	ALA129
B	SER130
B	SER133
B	LEU139
B	LEU197
B	THR198
B	THR199
B	ZN301
B	HOH610
B	HOH661
B	HOH662

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	WWX303

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 302

Chain	Residue
C	ASN64
C	HIS66
C	LYS69
C	WWX303

---

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE WWX C 303

Chain	Residue
C	TRP4
C	ASN64
C	SER67
C	THR88
C	GLN89
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	ALA129
C	SER133
C	LEU139
C	VAL141
C	LEU197
C	THR198
C	THR199
C	PRO200
C	PRO201
C	TRP208
C	ZN301
C	EDO302
C	HOH549

---

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

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	WWX305

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 302

Chain	Residue
D	SER42
D	THR44
D	LEU46
D	GLY80
D	TYR190
D	ARG192
D	HOH675

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 303

Chain	Residue
D	THR88
D	HOH588
D	ASN71
D	LEU72

---

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 304

Chain	Residue
D	ASP156
D	SER160
D	HOH626

---

site_id	BC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE WWX D 305

Chain	Residue
D	ASN64
D	SER67
D	GLN89
D	HIS91
D	HIS93
D	HIS117
D	VAL119
D	ALA129
D	SER130
D	SER133
D	LEU139
D	VAL141
D	LEU197
D	THR198
D	THR199
D	PRO200
D	PRO201
D	TRP208
D	ZN301
D	HOH500
D	HOH610
D	HOH629
D	HOH634
D	HOH670

---

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	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	HIS66
B	HIS66
C	HIS66
D	HIS66

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:11493685

Chain	Residue	Details
A	HIS91
D	HIS91
D	HIS93
D	HIS117
A	HIS93
A	HIS117
B	HIS91
B	HIS93
B	HIS117
C	HIS91
C	HIS93
C	HIS117

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	THR198
B	THR198
C	THR198
D	THR198

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN52
A	ASN134
B	ASN52
B	ASN134
C	ASN52
C	ASN134
D	ASN52
D	ASN134

---