Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HX3

Crystal structure of Streptomyces caespitosus sermetstatin in complex with S. caespitosus snapalysin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005576	cellular_component	extracellular region
B	0030414	molecular_function	peptidase inhibitor activity
B	0046872	molecular_function	metal ion binding
C	0004222	molecular_function	metalloendopeptidase activity
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0004867	molecular_function	serine-type endopeptidase inhibitor activity
D	0005576	cellular_component	extracellular region
D	0030414	molecular_function	peptidase inhibitor activity
D	0046872	molecular_function	metal ion binding
E	0004222	molecular_function	metalloendopeptidase activity
E	0005576	cellular_component	extracellular region
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0008237	molecular_function	metallopeptidase activity
E	0008270	molecular_function	zinc ion binding
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding
F	0004867	molecular_function	serine-type endopeptidase inhibitor activity
F	0005576	cellular_component	extracellular region
F	0030414	molecular_function	peptidase inhibitor activity
F	0046872	molecular_function	metal ion binding
G	0004222	molecular_function	metalloendopeptidase activity
G	0005576	cellular_component	extracellular region
G	0006508	biological_process	proteolysis
G	0008233	molecular_function	peptidase activity
G	0008237	molecular_function	metallopeptidase activity
G	0008270	molecular_function	zinc ion binding
G	0016787	molecular_function	hydrolase activity
G	0046872	molecular_function	metal ion binding
H	0004867	molecular_function	serine-type endopeptidase inhibitor activity
H	0005576	cellular_component	extracellular region
H	0030414	molecular_function	peptidase inhibitor activity
H	0046872	molecular_function	metal ion binding
I	0004222	molecular_function	metalloendopeptidase activity
I	0005576	cellular_component	extracellular region
I	0006508	biological_process	proteolysis
I	0008233	molecular_function	peptidase activity
I	0008237	molecular_function	metallopeptidase activity
I	0008270	molecular_function	zinc ion binding
I	0016787	molecular_function	hydrolase activity
I	0046872	molecular_function	metal ion binding
J	0004867	molecular_function	serine-type endopeptidase inhibitor activity
J	0005576	cellular_component	extracellular region
J	0030414	molecular_function	peptidase inhibitor activity
J	0046872	molecular_function	metal ion binding
K	0004222	molecular_function	metalloendopeptidase activity
K	0005576	cellular_component	extracellular region
K	0006508	biological_process	proteolysis
K	0008233	molecular_function	peptidase activity
K	0008237	molecular_function	metallopeptidase activity
K	0008270	molecular_function	zinc ion binding
K	0016787	molecular_function	hydrolase activity
K	0046872	molecular_function	metal ion binding
L	0004867	molecular_function	serine-type endopeptidase inhibitor activity
L	0005576	cellular_component	extracellular region
L	0030414	molecular_function	peptidase inhibitor activity
L	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 201

Chain	Residue
A	HIS83
A	HIS87
A	ASP93
A	HOH323

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 201

Chain	Residue
C	HIS83
C	HIS87
C	ASP93
C	HOH302

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 201

Chain	Residue
D	ALA41
D	PRO42
D	ARG43
D	ALA44
C	GLN96

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 201

Chain	Residue
E	HIS83
E	HIS87
E	ASP93
E	HOH309

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN G 201

Chain	Residue
G	HIS83
G	HIS87
G	ASP93
G	HOH311

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN I 201

Chain	Residue
I	HIS83
I	HIS87
I	ASP93
I	HOH312

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL J 501

Chain	Residue
D	GLN14
D	THR20
D	THR22
J	THR20
J	ASP21
J	HOH621

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN K 201

Chain	Residue
K	HIS83
K	HIS87
K	ASP93
K	HOH301

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9089404","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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