Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1U10

MEPA, active form with ZN in P1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000270	biological_process	peptidoglycan metabolic process
A	0004175	molecular_function	endopeptidase activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0000270	biological_process	peptidoglycan metabolic process
B	0004175	molecular_function	endopeptidase activity
B	0004222	molecular_function	metalloendopeptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008237	molecular_function	metallopeptidase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0009410	biological_process	response to xenobiotic stimulus
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
C	0000270	biological_process	peptidoglycan metabolic process
C	0004175	molecular_function	endopeptidase activity
C	0004222	molecular_function	metalloendopeptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008237	molecular_function	metallopeptidase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0009410	biological_process	response to xenobiotic stimulus
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
D	0000270	biological_process	peptidoglycan metabolic process
D	0004175	molecular_function	endopeptidase activity
D	0004222	molecular_function	metalloendopeptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008237	molecular_function	metallopeptidase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0009410	biological_process	response to xenobiotic stimulus
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding
E	0000270	biological_process	peptidoglycan metabolic process
E	0004175	molecular_function	endopeptidase activity
E	0004222	molecular_function	metalloendopeptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0008237	molecular_function	metallopeptidase activity
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0009410	biological_process	response to xenobiotic stimulus
E	0030288	cellular_component	outer membrane-bounded periplasmic space
E	0042597	cellular_component	periplasmic space
E	0046872	molecular_function	metal ion binding
F	0000270	biological_process	peptidoglycan metabolic process
F	0004175	molecular_function	endopeptidase activity
F	0004222	molecular_function	metalloendopeptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0006508	biological_process	proteolysis
F	0008233	molecular_function	peptidase activity
F	0008237	molecular_function	metallopeptidase activity
F	0009252	biological_process	peptidoglycan biosynthetic process
F	0009410	biological_process	response to xenobiotic stimulus
F	0030288	cellular_component	outer membrane-bounded periplasmic space
F	0042597	cellular_component	periplasmic space
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 400

Chain	Residue
A	HIS110
A	HIS113
A	ASP120
A	HIS211

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 500

Chain	Residue
A	GLN205
A	HIS206
A	ARG207
A	ALA208
A	HIS209

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 400

Chain	Residue
B	HIS110
B	HIS113
B	ASP120
B	HIS211

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	GLN205
B	HIS206
B	ARG207
B	ALA208
B	HIS209

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 400

Chain	Residue
C	HIS110
C	HIS113
C	ASP120
C	HIS211

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 502

Chain	Residue
C	GLN205
C	HIS206
C	ARG207
C	ALA208
C	HIS209

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 400

Chain	Residue
D	HIS110
D	HIS113
D	ASP120
D	HIS211

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 503

Chain	Residue
D	HIS206
D	ARG207
D	ALA208
D	HIS209

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 400

Chain	Residue
E	HIS110
E	HIS113
E	ASP120
E	HIS211

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 504

Chain	Residue
E	GLN205
E	HIS206
E	ARG207
E	ALA208
E	HIS209

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 400

Chain	Residue
F	HIS110
F	HIS113
F	ASP120
F	HIS211

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F 505

Chain	Residue
F	HIS206
F	ARG207
F	ALA208
F	HIS209

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 601

Chain	Residue
A	ASP147
A	HIS150
B	ASP147
B	HIS150

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 602

Chain	Residue
C	ASP147
C	HIS150
D	ASP147
D	HIS150

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 603

Chain	Residue
E	ASP147
E	HIS150
F	ASP147
F	HIS150

Functional Information from PROSITE/UniProt

site_id	PS00414
Number of Residues	9
Details	PROFILIN Profilin signature. aTpWQkItQ

Chain	Residue	Details
A	ALA20-GLN28

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:15292190

Chain	Residue	Details
A	HIS110
A	HIS113
A	ASP120
E	HIS110
E	HIS113
E	ASP120
E	ASP147
E	HIS150
E	HIS211
F	HIS110
F	HIS113
F	ASP120
F	ASP147
F	HIS150
F	HIS211
A	ASP147
A	HIS150
A	HIS211
B	HIS110
B	HIS113
B	ASP120
B	ASP147
B	HIS150
B	HIS211
C	HIS110
C	HIS113
C	ASP120
C	ASP147
C	HIS150
C	HIS211
D	HIS110
D	HIS113
D	ASP120
D	ASP147
D	HIS150
D	HIS211

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