Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZI6

Crystal structure of leucine aminopeptidase from Helicobacter pylori

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008235	molecular_function	metalloexopeptidase activity
A	0019538	biological_process	protein metabolic process
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008235	molecular_function	metalloexopeptidase activity
B	0019538	biological_process	protein metabolic process
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
B	0070006	molecular_function	metalloaminopeptidase activity
C	0004177	molecular_function	aminopeptidase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0008235	molecular_function	metalloexopeptidase activity
C	0019538	biological_process	protein metabolic process
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
C	0070006	molecular_function	metalloaminopeptidase activity
D	0004177	molecular_function	aminopeptidase activity
D	0005737	cellular_component	cytoplasm
D	0006508	biological_process	proteolysis
D	0008235	molecular_function	metalloexopeptidase activity
D	0019538	biological_process	protein metabolic process
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
D	0070006	molecular_function	metalloaminopeptidase activity
E	0004177	molecular_function	aminopeptidase activity
E	0005737	cellular_component	cytoplasm
E	0006508	biological_process	proteolysis
E	0008235	molecular_function	metalloexopeptidase activity
E	0019538	biological_process	protein metabolic process
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
E	0070006	molecular_function	metalloaminopeptidase activity
F	0004177	molecular_function	aminopeptidase activity
F	0005737	cellular_component	cytoplasm
F	0006508	biological_process	proteolysis
F	0008235	molecular_function	metalloexopeptidase activity
F	0019538	biological_process	protein metabolic process
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding
F	0070006	molecular_function	metalloaminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue ZN A 501

Chain	Residue
A	LYS258
A	ASP263
A	ASP281
A	GLU342
A	ZN502
A	HOH635
A	HOH812

site_id	AC2
Number of Residues	6
Details	binding site for residue ZN A 502

Chain	Residue
A	ASP340
A	GLU342
A	ZN501
A	HOH635
A	ASP263
A	LYS270

site_id	AC3
Number of Residues	7
Details	binding site for residue BCT A 503

Chain	Residue
A	LYS258
A	ALA341
A	GLU342
A	GLY343
A	ARG344
A	LEU368
A	HOH635

site_id	AC4
Number of Residues	6
Details	binding site for residue NA A 504

Chain	Residue
A	ALA461
A	GLY462
A	TYR465
A	HOH608
A	HOH652
A	HOH892

site_id	AC5
Number of Residues	8
Details	binding site for residue ZN B 501

Chain	Residue
B	LYS258
B	ASP263
B	ASP281
B	GLU342
B	ZN502
B	HOH683
B	HOH721
B	HOH813

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 502

Chain	Residue
B	ASP263
B	ASP340
B	GLU342
B	ZN501
B	HOH813

site_id	AC7
Number of Residues	8
Details	binding site for residue BCT B 503

Chain	Residue
B	LYS258
B	ALA341
B	GLU342
B	GLY343
B	ARG344
B	LEU368
B	HOH813
B	HOH820

site_id	AC8
Number of Residues	5
Details	binding site for residue NA B 504

Chain	Residue
B	ALA461
B	GLY462
B	TYR465
B	HOH614
B	HOH674

site_id	AC9
Number of Residues	8
Details	binding site for residue ZN C 501

Chain	Residue
C	LYS258
C	ASP263
C	ASP281
C	GLU342
C	ZN502
C	HOH648
C	HOH662
C	HOH848

site_id	AD1
Number of Residues	6
Details	binding site for residue ZN C 502

Chain	Residue
C	ASP263
C	ASP340
C	GLU342
C	ZN501
C	HOH648
C	HOH662

site_id	AD2
Number of Residues	7
Details	binding site for residue BCT C 503

Chain	Residue
C	LYS258
C	ALA341
C	GLU342
C	GLY343
C	ARG344
C	LEU368
C	HOH648

site_id	AD3
Number of Residues	6
Details	binding site for residue NA C 504

Chain	Residue
C	ALA461
C	GLY462
C	TYR465
C	HOH669
C	HOH748
C	HOH869

site_id	AD4
Number of Residues	8
Details	binding site for residue ZN D 501

Chain	Residue
D	LYS258
D	ASP263
D	ASP281
D	GLU342
D	ZN502
D	BCT503
D	HOH698
D	HOH852

site_id	AD5
Number of Residues	6
Details	binding site for residue ZN D 502

Chain	Residue
D	ASP263
D	LYS270
D	ASP340
D	GLU342
D	ZN501
D	HOH698

site_id	AD6
Number of Residues	8
Details	binding site for residue BCT D 503

Chain	Residue
D	ZN501
D	HOH698
D	LYS258
D	ALA341
D	GLU342
D	GLY343
D	ARG344
D	LEU368

site_id	AD7
Number of Residues	4
Details	binding site for residue NA D 504

Chain	Residue
D	ALA461
D	GLY462
D	TYR465
D	HOH676

site_id	AD8
Number of Residues	7
Details	binding site for residue ZN E 501

Chain	Residue
E	LYS258
E	ASP263
E	ASP281
E	GLU342
E	ZN502
E	HOH688
E	HOH853

site_id	AD9
Number of Residues	6
Details	binding site for residue ZN E 502

Chain	Residue
E	ASP263
E	ASP340
E	GLU342
E	ZN501
E	HOH688
E	HOH870

site_id	AE1
Number of Residues	7
Details	binding site for residue BCT E 503

Chain	Residue
E	LYS258
E	ALA341
E	GLU342
E	GLY343
E	ARG344
E	LEU368
E	HOH688

site_id	AE2
Number of Residues	6
Details	binding site for residue NA E 504

Chain	Residue
E	ALA461
E	GLY462
E	TYR465
E	HOH624
E	HOH637
E	HOH908

site_id	AE3
Number of Residues	7
Details	binding site for residue ZN F 501

Chain	Residue
F	LYS258
F	ASP263
F	ASP281
F	GLU342
F	ZN502
F	HOH727
F	HOH874

site_id	AE4
Number of Residues	5
Details	binding site for residue ZN F 502

Chain	Residue
F	ASP263
F	ASP340
F	GLU342
F	ZN501
F	HOH727

site_id	AE5
Number of Residues	7
Details	binding site for residue BCT F 503

Chain	Residue
F	LYS258
F	ALA341
F	GLU342
F	GLY343
F	ARG344
F	LEU368
F	HOH727

site_id	AE6
Number of Residues	4
Details	binding site for residue NA F 504

Chain	Residue
F	ALA461
F	GLY462
F	TYR465
F	HOH614

Functional Information from PROSITE/UniProt

site_id	PS00631
Number of Residues	8
Details	CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL

Chain	Residue	Details
A	ASN338-LEU345

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: ACT_SITE => ECO:0000255

Chain	Residue	Details
A	LYS270
A	ARG344
B	LYS270
B	ARG344
C	LYS270
C	ARG344
D	LYS270
D	ARG344
E	LYS270
E	ARG344
F	LYS270
F	ARG344

site_id	SWS_FT_FI2
Number of Residues	30
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
E	GLU342
F	LYS258
F	ASP263
F	ASP281
F	ASP340
F	GLU342
A	ASP340
A	GLU342
B	LYS258
B	ASP263
B	ASP281
B	ASP340
B	GLU342
C	LYS258
C	ASP263
C	ASP281
C	ASP340
C	GLU342
D	LYS258
D	ASP263
D	ASP281
D	ASP340
D	GLU342
E	LYS258
E	ASP263
E	ASP281
E	ASP340
A	LYS258
A	ASP263
A	ASP281

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