5MFT

The crystal structure of E. coli Aminopeptidase N in complex with 7-amino-1-bromo-4-phenyl-5,7,8,9-tetrahydrobenzocyclohepten-6-one

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	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0016285	molecular_function	alanyl aminopeptidase activity
A	0016787	molecular_function	hydrolase activity
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 1001

Chain	Residue
A	HIS297
A	HIS301
A	GLU320
A	7MF1002

---

site_id	AC2
Number of Residues	15
Details	binding site for residue 7MF A 1002

Chain	Residue
A	HIS297
A	GLU298
A	HIS301
A	LYS319
A	GLU320
A	TYR376
A	TYR381
A	ARG825
A	ZN1001
A	MLI1021
A	GLU121
A	MET260
A	ALA262
A	GLU264
A	ARG293

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NA A 1003

Chain	Residue
A	SER332
A	ASP333
A	GLY335
A	HOH2067
A	HOH2278
A	HOH2357

---

site_id	AC4
Number of Residues	6
Details	binding site for residue NA A 1004

Chain	Residue
A	HIS771
A	PHE774
A	HOH1493
A	HOH1551
A	HOH2270
A	HOH2325

---

site_id	AC5
Number of Residues	6
Details	binding site for residue NA A 1005

Chain	Residue
A	SER508
A	HOH2008
A	HOH2172
A	HOH2223
A	HOH2410
A	HOH2933

---

site_id	AC6
Number of Residues	6
Details	binding site for residue NA A 1006

Chain	Residue
A	ASP452
A	HOH1268
A	HOH1379
A	HOH2336
A	HOH2344
A	HOH2842

---

site_id	AC7
Number of Residues	7
Details	binding site for residue NA A 1007

Chain	Residue
A	GLU123
A	GLU371
A	HOH1153
A	HOH1298
A	HOH1682
A	HOH1693
A	HOH2373

---

site_id	AC8
Number of Residues	6
Details	binding site for residue NA A 1008

Chain	Residue
A	ASN399
A	SER429
A	HOH1595
A	HOH1658
A	HOH2035
A	HOH2246

---

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL A 1009

Chain	Residue
A	LEU61
A	VAL62
A	TRP74
A	ARG669
A	GLU671
A	HOH1126
A	HOH1871
A	HOH2079

---

site_id	AD1
Number of Residues	5
Details	binding site for residue GOL A 1010

Chain	Residue
A	ASN623
A	GLY791
A	HOH1113
A	HOH1253
A	HOH1625

---

site_id	AD2
Number of Residues	9
Details	binding site for residue GOL A 1011

Chain	Residue
A	PHE704
A	HIS705
A	ALA707
A	TYR735
A	LYS738
A	TRP739
A	HOH1161
A	HOH1559
A	HOH1832

---

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL A 1012

Chain	Residue
A	TRP74
A	LYS75
A	HOH1196
A	HOH1484
A	HOH1871
A	HOH2073

---

site_id	AD4
Number of Residues	11
Details	binding site for residue GOL A 1013

Chain	Residue
A	MET368
A	PRO473
A	ASP474
A	ALA476
A	HOH1110
A	HOH1357
A	HOH1629
A	HOH1755
A	HOH1758
A	HOH2084
A	HOH2105

---

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL A 1014

Chain	Residue
A	SER99
A	HOH1395
A	HOH2110
A	ASP58
A	LEU59
A	GLU97
A	ILE98

---

site_id	AD6
Number of Residues	13
Details	binding site for residue GOL A 1015

Chain	Residue
A	HIS11
A	ASP12
A	ARG14
A	ARG468
A	THR469
A	LYS478
A	GLN479
A	HOH1179
A	HOH1191
A	HOH1805
A	HOH1875
A	HOH2322
A	HOH2822

---

site_id	AD7
Number of Residues	8
Details	binding site for residue GOL A 1016

Chain	Residue
A	LYS541
A	GLU627
A	PHE629
A	ASP630
A	ARG835
A	HOH1261
A	HOH1276
A	HOH2128

---

site_id	AD8
Number of Residues	6
Details	binding site for residue DMS A 1017

Chain	Residue
A	THR393
A	LEU394
A	LEU395
A	GLY396
A	ASN507
A	HOH1782

---

site_id	AD9
Number of Residues	3
Details	binding site for residue DMS A 1018

Chain	Residue
A	THR393
A	GLU535
A	HOH1157

---

site_id	AE1
Number of Residues	5
Details	binding site for residue CL A 1019

Chain	Residue
A	ASP216
A	ASN219
A	ALA254
A	SER273
A	HOH1698

---

site_id	AE2
Number of Residues	4
Details	binding site for residue CL A 1020

Chain	Residue
A	ALA31
A	GLN32
A	HOH1490
A	HOH2131

---

site_id	AE3
Number of Residues	9
Details	binding site for residue MLI A 1021

Chain	Residue
A	TYR376
A	THR377
A	LEU378
A	TYR381
A	GLU382
A	ARG825
A	7MF1002
A	HOH1115
A	HOH1224

---

site_id	AE4
Number of Residues	11
Details	binding site for residue MLI A 1022

Chain	Residue
A	GLY396
A	GLU397
A	GLU398
A	HOH1119
A	HOH1204
A	HOH1246
A	HOH1591
A	HOH1763
A	HOH1996
A	HOH2136
A	HOH2576

---

site_id	AE5
Number of Residues	10
Details	binding site for residue MLI A 1023

Chain	Residue
A	ALA531
A	LEU532
A	TRP546
A	LEU551
A	LEU554
A	ASP566
A	ALA567
A	SER570
A	HOH1105
A	HOH1714

---

site_id	AE6
Number of Residues	10
Details	binding site for residue MLI A 1024

Chain	Residue
A	LYS8
A	GLU123
A	TRP313
A	PHE314
A	VAL369
A	MET372
A	HOH1153
A	HOH1181
A	HOH1271
A	HOH1600

---

site_id	AE7
Number of Residues	7
Details	binding site for residue MLI A 1025

Chain	Residue
A	ASP28
A	LEU29
A	ASP30
A	LYS33
A	ARG171
A	HOH1205
A	HOH2131

---

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	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16885166","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18416562","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19622865","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---