3FVL

Crystallogic studies on the Complex of Carboxypeptidase A with inhibitors using alpha-hydroxy ketone as zinc-binding group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0006508	biological_process	proteolysis
A	0008270	molecular_function	zinc ion binding
C	0004181	molecular_function	metallocarboxypeptidase activity
C	0006508	biological_process	proteolysis
C	0008270	molecular_function	zinc ion binding
E	0004181	molecular_function	metallocarboxypeptidase activity
E	0006508	biological_process	proteolysis
E	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A1309

Chain	Residue
A	HIS69
A	GLU72
A	HIS196
A	BHK311

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site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BHK A 311

Chain	Residue
A	HIS196
A	TYR248
A	ALA250
A	SER251
A	GLY253
A	GLU270
A	ZN1309
A	HIS69
A	GLU72
A	ARG127
A	ASN144
A	ARG145

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C1309

Chain	Residue
C	HIS69
C	GLU72
C	HIS196
C	BHK311

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BHK C 311

Chain	Residue
C	HIS69
C	GLU72
C	ARG127
C	ASN144
C	ARG145
C	HIS196
C	SER197
C	ILE243
C	ALA250
C	GLU270
C	PHE279
C	HOH480
C	ZN1309

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E1309

Chain	Residue
E	HIS69
E	GLU72
E	HIS196
E	BHK311

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BHK E 311

Chain	Residue
E	HIS69
E	GLU72
E	ARG127
E	ASN144
E	ARG145
E	HIS196
E	TYR248
E	ALA250
E	GLY253
E	GLU270
E	PHE279
E	ZN1309

---

Functional Information from PROSITE/UniProt

site_id	PS00132
Number of Residues	23
Details	CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PaIwIdlGiHSrEwITQatgvwF

Chain	Residue	Details
A	PRO60-PHE82

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site_id	PS00133
Number of Residues	11
Details	CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HSYSQLLlYPY

Chain	Residue	Details
A	HIS196-TYR206

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379

Chain	Residue	Details
A	GLU270
C	GLU270
E	GLU270

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7

Chain	Residue	Details
A	HIS69
A	GLU72
A	HIS196
C	HIS69
C	GLU72
C	HIS196
E	HIS69
E	GLU72
E	HIS196

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:12431056, ECO:0007744|PDB:1IY7

Chain	Residue	Details
A	ARG127
E	ASN144
E	SER197
E	TYR248
A	ASN144
A	SER197
A	TYR248
C	ARG127
C	ASN144
C	SER197
C	TYR248
E	ARG127

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 171

Chain	Residue	Details
A	HIS69	metal ligand
A	GLU72	metal ligand
A	ARG127	electrostatic stabiliser, hydrogen bond donor
A	HIS196	metal ligand
A	GLU270	covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 171

Chain	Residue	Details
C	HIS69	metal ligand
C	GLU72	metal ligand
C	ARG127	electrostatic stabiliser, hydrogen bond donor
C	HIS196	metal ligand
C	GLU270	covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 171

Chain	Residue	Details
E	HIS69	metal ligand
E	GLU72	metal ligand
E	ARG127	electrostatic stabiliser, hydrogen bond donor
E	HIS196	metal ligand
E	GLU270	covalently attached, electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleophile, proton acceptor, proton donor

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