3NDV

Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with ampicillin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0042597	cellular_component	periplasmic space
A	0042802	molecular_function	identical protein binding
B	0004177	molecular_function	aminopeptidase activity
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0016787	molecular_function	hydrolase activity
B	0042597	cellular_component	periplasmic space
B	0042802	molecular_function	identical protein binding
C	0004177	molecular_function	aminopeptidase activity
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0016787	molecular_function	hydrolase activity
C	0042597	cellular_component	periplasmic space
C	0042802	molecular_function	identical protein binding
D	0004177	molecular_function	aminopeptidase activity
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0016787	molecular_function	hydrolase activity
D	0042597	cellular_component	periplasmic space
D	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 374

Chain	Residue
A	VAL88
C	ASP315
A	GLY89
A	GLN90
A	PRO263
A	HIS299
A	ILE301
A	PRO307
C	MET262
C	HIS264

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AIC A 375

Chain	Residue
A	THR76
A	GLU133
A	THR134
A	LEU135
A	ARG138
A	SER250
A	LEU287
A	SER288
A	NDV376
A	HOH390
A	HOH628
B	PHE124

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NDV A 376

Chain	Residue
A	ARG138
A	VAL232
A	ALA237
A	ALA238
A	AIC375

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 374

Chain	Residue
B	VAL88
B	GLY89
B	GLN90
B	PRO263
B	HIS299
B	ILE301
B	PRO307
D	MET262
D	HIS264
D	ASP315

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL B 375

Chain	Residue
B	MET262
B	HIS264
B	ASP315
D	VAL88
D	GLY89
D	GLN90
D	PRO263
D	HIS299
D	ILE301
D	PRO307

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AIC B 376

Chain	Residue
A	PHE124
B	THR76
B	GLY77
B	GLU133
B	LEU135
B	ASN137
B	ARG138
B	SER250
B	LEU287
B	SER288
B	HOH400
B	HOH930

---

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 374

Chain	Residue
A	MET262
A	HIS264
A	ASP315
C	VAL88
C	GLY89
C	GLN90
C	PRO263
C	HIS299
C	ILE301
C	PRO307

---

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AIC C 375

Chain	Residue
C	THR76
C	GLY77
C	GLU133
C	LEU135
C	ASN137
C	ARG138
C	SER250
C	LEU287
C	HOH386
C	HOH836
C	HOH950
D	PHE124

---

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AIC D 374

Chain	Residue
C	PHE124
D	THR76
D	GLY77
D	GLU133
D	LEU135
D	ARG138
D	SER250
D	LEU287
D	SER288
D	NDV375
D	HOH396
D	HOH708

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NDV D 375

Chain	Residue
D	ARG138
D	VAL232
D	ALA237
D	ALA238
D	AIC374

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"22980995","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22980995","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---