Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GL1

structure of the complex between bovine alpha-chymotrypsin and PMP-C, an inhibitor from the insect Locusta migratoria

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0007586	biological_process	digestion
A	0008236	molecular_function	serine-type peptidase activity
A	0097180	cellular_component	serine protease inhibitor complex
A	0097655	molecular_function	serpin family protein binding
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0006508	biological_process	proteolysis
B	0007586	biological_process	digestion
B	0008236	molecular_function	serine-type peptidase activity
B	0097180	cellular_component	serine protease inhibitor complex
B	0097655	molecular_function	serpin family protein binding
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0007586	biological_process	digestion
C	0008236	molecular_function	serine-type peptidase activity
C	0097180	cellular_component	serine protease inhibitor complex
C	0097655	molecular_function	serpin family protein binding
I	0030414	molecular_function	peptidase inhibitor activity
J	0030414	molecular_function	peptidase inhibitor activity
K	0030414	molecular_function	peptidase inhibitor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD A1246

Chain	Residue
A	ASN245
A	HOH2103
C	ASP128
C	HOH2060
C	HOH2066

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A1247

Chain	Residue
A	ASP72
A	ASP153
A	ASP178
A	HOH2070

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD B1246

Chain	Residue
A	ASP128
A	HOH2057
B	ASN245
B	HOH2028
B	HOH2121

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B1247

Chain	Residue
B	ASP72
B	ASP153
B	ASP178
B	HOH2040

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD C1246

Chain	Residue
B	ASP129
C	ASN245
C	HOH2028
C	HOH2129

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD C1247

Chain	Residue
C	ASP72
C	ASP153
C	ASP178
C	HOH2085

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC

Chain	Residue	Details
A	VAL53-CYS58

site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV

Chain	Residue	Details
A	SER189-VAL200

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	SITE: Reactive bond

Chain	Residue	Details
I	LEU30
J	LEU30
K	LEU30
B	HIS57
B	ASP102
B	SER195
C	HIS57
C	ASP102
C	SER195

site_id	SWS_FT_FI2
Number of Residues	3
Details	CARBOHYD: O-linked (Fuc) threonine => ECO:0000269\|PubMed:8613985

Chain	Residue	Details
I	THR9
J	THR9
K	THR9

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	GLY193
A	HIS57

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	GLY193
B	HIS57

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	GLY193
C	HIS57

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57
A	GLY196

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57
B	GLY196

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57
C	GLY196

site_id	MCSA1
Number of Residues	5
Details	M-CSA 387

Chain	Residue	Details
A	HIS57	electrostatic stabiliser, proton shuttle (general acid/base)
A	ASP102	modifies pKa
A	GLY193	electrostatic stabiliser
A	SER195	covalent catalysis
A	GLY196	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 387

Chain	Residue	Details
B	HIS57	electrostatic stabiliser, proton shuttle (general acid/base)
B	ASP102	modifies pKa
B	GLY193	electrostatic stabiliser
B	SER195	covalent catalysis
B	GLY196	electrostatic stabiliser

site_id	MCSA3
Number of Residues	5
Details	M-CSA 387

Chain	Residue	Details
C	HIS57	electrostatic stabiliser, proton shuttle (general acid/base)
C	ASP102	modifies pKa
C	GLY193	electrostatic stabiliser
C	SER195	covalent catalysis
C	GLY196	electrostatic stabiliser

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