Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3E2W

H. influenzae beta-carbonic anhydrase, variant Y181F with 1M bicarbonate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005575	cellular_component	cellular_component
A	0008270	molecular_function	zinc ion binding
A	0015976	biological_process	carbon utilization
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0005575	cellular_component	cellular_component
B	0008270	molecular_function	zinc ion binding
B	0015976	biological_process	carbon utilization
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0005575	cellular_component	cellular_component
C	0008270	molecular_function	zinc ion binding
C	0015976	biological_process	carbon utilization
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
D	0004089	molecular_function	carbonate dehydratase activity
D	0005575	cellular_component	cellular_component
D	0008270	molecular_function	zinc ion binding
D	0015976	biological_process	carbon utilization
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
E	0004089	molecular_function	carbonate dehydratase activity
E	0005575	cellular_component	cellular_component
E	0008270	molecular_function	zinc ion binding
E	0015976	biological_process	carbon utilization
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
F	0004089	molecular_function	carbonate dehydratase activity
F	0005575	cellular_component	cellular_component
F	0008270	molecular_function	zinc ion binding
F	0015976	biological_process	carbon utilization
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 230

Chain	Residue
A	CYS42
A	ASP44
A	HIS98
A	CYS101

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 231

Chain	Residue
A	LEU121
A	ARG124
A	HOH277
B	ARG160
B	ARG198

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 232

Chain	Residue
A	ARG160
A	ARG198
B	LEU121
B	ARG124

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 233

Chain	Residue
A	ARG46
A	VAL47
A	HIS98
A	PHE181
A	VAL183
A	HOH267

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 230

Chain	Residue
B	CYS42
B	ASP44
B	HIS98
B	CYS101

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 231

Chain	Residue
B	SER45
B	ARG46
B	VAL47
B	HIS98
B	PHE181
B	VAL183

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 230

Chain	Residue
C	CYS42
C	ASP44
C	HIS98
C	CYS101

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 231

Chain	Residue
C	SER45
C	ARG46
C	HIS98
C	VAL183

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 230

Chain	Residue
D	CYS42
D	ASP44
D	HIS98
D	CYS101

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 231

Chain	Residue
C	LEU121
C	ARG124
D	ARG160
D	ARG198

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 232

Chain	Residue
C	ARG160
C	ARG198
D	LEU121
D	ARG124

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 233

Chain	Residue
D	ARG46
D	VAL47
D	HIS98
D	PHE181
D	VAL183
D	HOH250

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 230

Chain	Residue
E	CYS42
E	ASP44
E	HIS98
E	CYS101

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 231

Chain	Residue
E	LEU121
E	ARG124
F	ARG160
F	ARG198

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 232

Chain	Residue
E	ARG46
E	VAL47
E	HIS98
E	PHE181
E	VAL183

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 230

Chain	Residue
F	CYS42
F	ASP44
F	HIS98
F	CYS101

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCT F 231

Chain	Residue
D	ARG64
F	PRO48
F	ALA49
F	GLU50
F	ARG64
F	HOH269
F	HOH274

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 232

Chain	Residue
E	ARG160
E	ARG198
F	ARG124

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 233

Chain	Residue
F	ASP44
F	SER45
F	ARG46
F	HIS98
F	PHE181
F	VAL183

Functional Information from PROSITE/UniProt

site_id	PS00704
Number of Residues	8
Details	PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVpA

Chain	Residue	Details
A	CYS42-ALA49

site_id	PS00705
Number of Residues	21
Details	PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLkiehIIIcGHtnCG

Chain	Residue	Details
A	GLN82-GLY102

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:16584170, ECO:0007744\|PDB:2A8C, ECO:0007744\|PDB:2A8D

Chain	Residue	Details
A	CYS42
A	ASP44
E	HIS98
E	CYS101
F	CYS42
F	ASP44
F	HIS98
F	CYS101
A	HIS98
A	CYS101
B	CYS42
B	ASP44
B	HIS98
B	CYS101
C	CYS42
C	ASP44
C	HIS98
C	CYS101
D	CYS42
D	ASP44
D	HIS98
D	CYS101
E	CYS42
E	ASP44

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)