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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5LL9

Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide

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	6YQ302

site_id	AC2
Number of Residues	15
Details	binding site for residue 6YQ A 302

Chain	Residue
A	VAL141
A	LEU197
A	THR198
A	THR199
A	PRO201
A	TRP208
A	ZN301
A	EDO303
A	EDO304
A	HOH429
A	HIS91
A	HIS93
A	HIS117
A	SER130
A	SER133

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 303

Chain	Residue
A	ASN64
A	HIS66
A	GLN89
A	6YQ302
A	EDO304
A	HOH593

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 304

Chain	Residue
A	ASN64
A	LYS69
A	GLN89
A	6YQ302
A	EDO303

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 305

Chain	Residue
A	ASP156
A	SER160
A	HOH463

site_id	AC6
Number of Residues	6
Details	binding site for residue EDO A 306

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

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

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	6YQ302

site_id	AC8
Number of Residues	14
Details	binding site for residue 6YQ B 302

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	SER130
B	VAL141
B	LEU197
B	THR198
B	THR199
B	PRO201
B	TRP208
B	ZN301
B	SO4303
B	EDO304
B	HOH408

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 B 303

Chain	Residue
B	ASN64
B	LYS69
B	6YQ302
B	EDO304
B	HOH408

site_id	AD1
Number of Residues	8
Details	binding site for residue EDO B 304

Chain	Residue
B	ASN64
B	HIS66
B	GLN89
B	HIS91
B	6YQ302
B	SO4303
B	HOH452
B	HOH559

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO B 305

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

site_id	AD3
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	6YQ302

site_id	AD4
Number of Residues	13
Details	binding site for residue 6YQ C 302

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	SER130
C	SER133
C	VAL141
C	LEU197
C	THR198
C	THR199
C	PRO201
C	TRP208
C	ZN301
C	SO4303

site_id	AD5
Number of Residues	5
Details	binding site for residue SO4 C 303

Chain	Residue
C	ASN64
C	LYS69
C	6YQ302
C	EDO305
C	HOH564

site_id	AD6
Number of Residues	7
Details	binding site for residue EDO C 304

Chain	Residue
C	GLY80
C	LEU81
C	TYR190
C	ARG192
C	HOH414
C	SER42
C	LEU46

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO C 305

Chain	Residue
C	ASN64
C	HIS66
C	GLN89
C	HIS91
C	SO4303
C	HOH564

site_id	AD8
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	6YQ302

site_id	AD9
Number of Residues	12
Details	binding site for residue 6YQ D 302

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	SER130
D	VAL141
D	LEU197
D	THR198
D	THR199
D	PRO201
D	TRP208
D	ZN301
D	SO4303

site_id	AE1
Number of Residues	5
Details	binding site for residue SO4 D 303

Chain	Residue
D	ASN64
D	LYS69
D	6YQ302
D	EDO304
D	HOH464

site_id	AE2
Number of Residues	7
Details	binding site for residue EDO D 304

Chain	Residue
D	ASN64
D	HIS66
D	GLN89
D	HIS91
D	SO4303
D	HOH402
D	HOH487

site_id	AE3
Number of Residues	8
Details	binding site for residue EDO D 305

Chain	Residue
D	SER42
D	THR44
D	LEU46
D	GLY80
D	TYR190
D	ARG192
D	HOH410
D	HOH584

site_id	AE4
Number of Residues	7
Details	binding site for residue EDO D 306

Chain	Residue
D	GLU180
D	GLU181
D	LEU183
D	HOH431
D	HOH442
D	HOH498
D	HOH557

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

221051

PDB entries from 2024-06-12

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