Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4A94

Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4

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
B	0004181	molecular_function	metallocarboxypeptidase activity
B	0006508	biological_process	proteolysis
B	0008270	molecular_function	zinc ion binding
C	0004857	molecular_function	enzyme inhibitor activity
C	0008191	molecular_function	metalloendopeptidase inhibitor activity
C	0010951	biological_process	negative regulation of endopeptidase activity
C	0030414	molecular_function	peptidase inhibitor activity
C	0046872	molecular_function	metal ion binding
D	0004857	molecular_function	enzyme inhibitor activity
D	0008191	molecular_function	metalloendopeptidase inhibitor activity
D	0010951	biological_process	negative regulation of endopeptidase activity
D	0030414	molecular_function	peptidase inhibitor activity
D	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 500

Chain	Residue
A	HIS69
A	GLU72
A	HIS196
D	ALA53

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 A 1309

Chain	Residue
A	TYR248
A	GLU270
D	ALA53
A	HIS69
A	ARG127
A	ASN144
A	ARG145
A	HIS196

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 A 1310

Chain	Residue
A	ARG71
A	LEU125
A	TRP126
A	ARG127
A	LYS128
A	HOH2094

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 501

Chain	Residue
B	HIS69
B	GLU72
B	HIS196
C	ALA53

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 B 1309

Chain	Residue
B	HIS69
B	ARG127
B	ASN144
B	ARG145
B	TYR248
B	GLU270
C	ALA53

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 B 1310

Chain	Residue
B	LEU125
B	TRP126
B	ARG127
B	LYS128
B	GLU163
B	HOH2035
B	HOH2039
C	GLN39

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 C 1054

Chain	Residue
B	ASN159
B	CYS161
C	ARG7
C	ILE10
C	PHE25
C	HIS40

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 D 1054

Chain	Residue
A	ASN159
A	CYS161
D	ARG7
D	CYS9
D	ILE10
D	PHE25
D	HIS40

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO60-THR82

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

Chain	Residue	Details
A	HIS196-TYR206

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	588
Details	Domain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15738388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16091843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22294694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23746805","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BD9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15738388","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16091843","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17506531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2BO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2PCU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22294694","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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