1BCS

COMPLEX OF THE WHEAT SERINE CARBOXYPEPTIDASE, CPDW-II, WITH THE MICROBIAL PEPTIDE ALDEHYDE INHIBITOR, CHYMOSTATIN, AND ARGININE AT 100 DEGREES KELVIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004185	molecular_function	serine-type carboxypeptidase activity
A	0006508	biological_process	proteolysis
B	0004185	molecular_function	serine-type carboxypeptidase activity
B	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	CAT
Number of Residues	3
Details	THREE RESIDUES FORMING THE CATALYTIC CENTER

Chain	Residue
B	ASP338
B	HIS397
A	SER146

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Functional Information from PROSITE/UniProt

site_id	PS00131
Number of Residues	8
Details	CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG

Chain	Residue	Details
A	ILE142-GLY149

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site_id	PS00560
Number of Residues	18
Details	CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. LtlVsVrGAGHeVPlhrP

Chain	Residue	Details
B	LEU387-PRO404

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PubMed","id":"8636973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7727364","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BCS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WHS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WHT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1390755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7727364","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8636973","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WHT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SC2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7727364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WHT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1bcr

Chain	Residue	Details
A	GLY53
A	TYR147
A	SER146
B	ASP338
B	HIS397

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 5

Chain	Residue	Details
B	ASP338	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
B	HIS397	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR147	electrostatic stabiliser, hydrogen bond donor

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