1WHS

STRUCTURE OF THE COMPLEX OF L-BENZYLSUCCINATE WITH WHEAT SERINE CARBOXYPEPTIDASE II AT 2.0 ANGSTROMS RESOLUTION

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	ACT
Number of Residues	4
Details

Chain	Residue
B	ASP338
B	HIS397
A	SER146
A	GLU145

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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	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR

Chain	Residue	Details
B	THR367
B	LYS418

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:7727364, ECO:0007744|PDB:1WHT

Chain	Residue	Details
B	PHE414
A	GLU145

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:1390755, ECO:0000269|PubMed:7727364, ECO:0000269|PubMed:8636973, ECO:0007744|PDB:1BCR, ECO:0007744|PDB:1WHT, ECO:0007744|PDB:3SC2

Chain	Residue	Details
B	HIS308
A	ASN113

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
B	MET313

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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	THR367	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
B	LYS418	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR147	electrostatic stabiliser, hydrogen bond donor

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