Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KBW

CRYSTAL STRUCTURE OF THE SOLUBLE DOMAIN OF ANIA FROM NEISSERIA GONORRHOEAE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0006807	biological_process	obsolete nitrogen compound metabolic process
A	0050421	molecular_function	nitrite reductase (NO-forming) activity
B	0005507	molecular_function	copper ion binding
B	0006807	biological_process	obsolete nitrogen compound metabolic process
B	0050421	molecular_function	nitrite reductase (NO-forming) activity
C	0005507	molecular_function	copper ion binding
C	0006807	biological_process	obsolete nitrogen compound metabolic process
C	0050421	molecular_function	nitrite reductase (NO-forming) activity
D	0005507	molecular_function	copper ion binding
D	0006807	biological_process	obsolete nitrogen compound metabolic process
D	0050421	molecular_function	nitrite reductase (NO-forming) activity
E	0005507	molecular_function	copper ion binding
E	0006807	biological_process	obsolete nitrogen compound metabolic process
E	0050421	molecular_function	nitrite reductase (NO-forming) activity
F	0005507	molecular_function	copper ion binding
F	0006807	biological_process	obsolete nitrogen compound metabolic process
F	0050421	molecular_function	nitrite reductase (NO-forming) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 501

Chain	Residue
A	HIS94
A	CYS135
A	HIS143
A	MET148

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 502

Chain	Residue
A	ASP97
A	HIS99
A	HIS134
B	HIS289
B	HOH682

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU B 501

Chain	Residue
B	HIS94
B	CYS135
B	HIS143
B	MET148

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 502

Chain	Residue
B	ASP97
B	HIS99
B	HIS134
B	HOH683
C	HIS289

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 501

Chain	Residue
C	HIS94
C	CYS135
C	HIS143
C	MET148

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CU C 502

Chain	Residue
A	HIS240
A	HIS289
A	HOH696
C	ASP97
C	HIS99
C	HIS134
C	HOH682

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU D 501

Chain	Residue
D	HIS94
D	CYS135
D	HIS143
D	MET148

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU D 502

Chain	Residue
D	ASP97
D	HIS99
D	HIS134
D	HOH710
E	HIS240
E	HIS289

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU E 501

Chain	Residue
E	HIS94
E	CYS135
E	HIS143
E	MET148

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU E 502

Chain	Residue
E	HIS99
E	HIS134
E	HOH693
F	HIS289

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU F 501

Chain	Residue
F	HIS94
F	CYS135
F	HIS143
F	MET148

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU F 502

Chain	Residue
D	HIS240
D	HIS289
F	HIS99
F	HIS134
F	HOH657
F	HOH658

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: type 1 copper site

Chain	Residue	Details
A	HIS94
C	CYS135
C	HIS143
C	MET148
D	HIS94
D	CYS135
D	HIS143
D	MET148
E	HIS94
E	CYS135
E	HIS143
A	CYS135
E	MET148
F	HIS94
F	CYS135
F	HIS143
F	MET148
A	HIS143
A	MET148
B	HIS94
B	CYS135
B	HIS143
B	MET148
C	HIS94

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11827480

Chain	Residue	Details
A	HIS99
E	HIS240
F	HIS99
F	HIS240
A	HIS240
B	HIS99
B	HIS240
C	HIS99
C	HIS240
D	HIS99
D	HIS240
E	HIS99

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: type 2 copper site

Chain	Residue	Details
A	HIS134
E	HIS289
F	HIS134
F	HIS289
A	HIS289
B	HIS134
B	HIS289
C	HIS134
C	HIS289
D	HIS134
D	HIS289
E	HIS134

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
F	GLY65
F	PHE63

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
A	GLY65
A	PHE63

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
D	GLY65
D	PHE63

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
C	GLY65
C	PHE63

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
E	GLY65
E	PHE63

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
B	GLY65
B	PHE63

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
A	ASP97
A	HIS240

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
B	ASP97
B	HIS240

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
C	ASP97
C	HIS240

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
D	ASP97
D	HIS240

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
E	ASP97
E	HIS240

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1nid

Chain	Residue	Details
F	ASP97
F	HIS240

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)