4XO3

Crystal Structure of E. coli Aminopeptidase N in complex with L-Leucine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0042802	molecular_function	identical protein binding
A	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 901

Chain	Residue
A	HIS297
A	HIS301
A	GLU320
A	LEU902

---

site_id	AC2
Number of Residues	17
Details	binding site for residue LEU A 902

Chain	Residue
A	GLU264
A	HIS297
A	GLU298
A	HIS301
A	LYS319
A	GLU320
A	TYR376
A	TYR381
A	ZN901
A	MLI917
A	HOH1338
A	HOH1512
A	GLN119
A	GLU121
A	MET260
A	ALA262
A	MET263

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 903

Chain	Residue
A	SER332
A	ASP333
A	GLY335
A	HOH1643
A	HOH1830
A	HOH1907

---

site_id	AC4
Number of Residues	5
Details	binding site for residue NA A 904

Chain	Residue
A	ASP452
A	NA909
A	HOH1721
A	HOH1881
A	HOH1900

---

site_id	AC5
Number of Residues	6
Details	binding site for residue NA A 905

Chain	Residue
A	HIS771
A	PHE774
A	HOH1198
A	HOH1543
A	HOH1760
A	HOH1921

---

site_id	AC6
Number of Residues	5
Details	binding site for residue NA A 906

Chain	Residue
A	ALA102
A	HOH1147
A	HOH1798
A	HOH1864
A	HOH2151

---

site_id	AC7
Number of Residues	5
Details	binding site for residue NA A 907

Chain	Residue
A	TYR544
A	HOH1534
A	HOH1752
A	HOH1869
A	HOH2046

---

site_id	AC8
Number of Residues	7
Details	binding site for residue NA A 908

Chain	Residue
A	GLU123
A	GLU371
A	HOH1117
A	HOH1353
A	HOH1517
A	HOH1627
A	HOH1888

---

site_id	AC9
Number of Residues	7
Details	binding site for residue NA A 909

Chain	Residue
A	ASP452
A	TYR544
A	NA904
A	HOH1317
A	HOH1832
A	HOH1900
A	HOH1916

---

site_id	AD1
Number of Residues	5
Details	binding site for residue NA A 910

Chain	Residue
A	GLU426
A	ASP432
A	SER434
A	HOH1320
A	HOH1901

---

site_id	AD2
Number of Residues	5
Details	binding site for residue NA A 911

Chain	Residue
A	GLN19
A	ILE20
A	LEU138
A	HOH1761
A	HOH1963

---

site_id	AD3
Number of Residues	6
Details	binding site for residue NA A 912

Chain	Residue
A	TYR131
A	LEU132
A	ARG134
A	VAL137
A	PRO183
A	CYS184

---

site_id	AD4
Number of Residues	5
Details	binding site for residue NA A 913

Chain	Residue
A	GLN164
A	TYR454
A	HOH1014
A	HOH1568
A	HOH1772

---

site_id	AD5
Number of Residues	5
Details	binding site for residue GOL A 914

Chain	Residue
A	MET260
A	TYR376
A	GLU382
A	ARG825
A	HOH1157

---

site_id	AD6
Number of Residues	11
Details	binding site for residue MLI A 915

Chain	Residue
A	ARG641
A	GLU642
A	THR645
A	ARG686
A	ALA722
A	HOH1086
A	HOH1186
A	HOH1267
A	HOH1658
A	HOH1664
A	HOH1746

---

site_id	AD7
Number of Residues	8
Details	binding site for residue MLI A 916

Chain	Residue
A	ASN259
A	LYS274
A	ASN780
A	ARG783
A	HOH1038
A	HOH1075
A	HOH1171
A	HOH1679

---

site_id	AD8
Number of Residues	8
Details	binding site for residue MLI A 917

Chain	Residue
A	ARG293
A	HIS297
A	GLU298
A	ASP327
A	TYR381
A	LEU902
A	HOH1385
A	HOH1512

---

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW

Chain	Residue	Details
A	VAL294-TRP303

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:16885166, ECO:0000305|PubMed:18416562, ECO:0000305|PubMed:19622865

Chain	Residue	Details
A	GLU298

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	GLU121
A	GLY261
A	HIS297
A	HIS301
A	GLU320

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305

Chain	Residue	Details
A	TYR381

---