4KP5

Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with 2-Chloro-4-[(pyrimidin-2-ylsulfanyl)acetyl]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	E1F302

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE E1F A 302

Chain	Residue
A	LEU197
A	THR198
A	THR199
A	PRO201
A	TRP208
A	ZN301
A	EDO303
A	HOH670
A	HIS91
A	HIS93
A	HIS117
A	SER133
A	VAL141

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	ASN64
A	HIS66
A	GLN89
A	HIS91
A	E1F302
A	HOH666
A	HOH670

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 304

Chain	Residue
A	ASP156
A	SER160
A	GLN221
A	HOH564

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	E1F302

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE E1F B 302

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	SER133
B	VAL141
B	LEU197
B	THR198
B	THR199
B	PRO201
B	ASN203
B	TRP208
B	ZN301

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 303

Chain	Residue
B	ASN64
B	GLN89
B	HIS91
B	HOH430
B	HOH489

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 304

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

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	E1F302

---

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE E1F C 302

Chain	Residue
C	GLN89
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	SER133
C	VAL141
C	LEU197
C	THR198
C	THR199
C	PRO201
C	TRP208
C	ZN301
C	HOH581

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 303

Chain	Residue
C	SER218
C	GLN219
C	GLU220
C	HOH576
C	HOH624

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	E1F302

---

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE E1F D 302

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	SER130
D	SER133
D	VAL141
D	LEU197
D	THR198
D	PRO201
D	TRP208
D	ZN301
D	EDO303
D	HOH678

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 303

Chain	Residue
D	HOH678
D	ASN64
D	HIS66
D	GLN89
D	HIS91
D	E1F302

---

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 304

Chain	Residue
D	SER42
D	THR44
D	LEU46
D	GLY80
D	TYR190
D	ARG192
D	HOH713

---

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
A	HIS93
A	HIS117
B	HIS91
B	HIS93
B	HIS117
C	HIS91
C	HIS93
C	HIS117
D	HIS91
D	HIS93
D	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

---