Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KXQ

Camelid VHH Domain in Complex with Porcine Pancreatic alpha-Amylase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004556	molecular_function	alpha-amylase activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005975	biological_process	carbohydrate metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016160	molecular_function	amylase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031404	molecular_function	chloride ion binding
A	0043169	molecular_function	cation binding
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004556	molecular_function	alpha-amylase activity
B	0005509	molecular_function	calcium ion binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005975	biological_process	carbohydrate metabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016160	molecular_function	amylase activity
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0031404	molecular_function	chloride ion binding
B	0043169	molecular_function	cation binding
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0004556	molecular_function	alpha-amylase activity
C	0005509	molecular_function	calcium ion binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005975	biological_process	carbohydrate metabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016160	molecular_function	amylase activity
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0031404	molecular_function	chloride ion binding
C	0043169	molecular_function	cation binding
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0004556	molecular_function	alpha-amylase activity
D	0005509	molecular_function	calcium ion binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005975	biological_process	carbohydrate metabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016160	molecular_function	amylase activity
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0031404	molecular_function	chloride ion binding
D	0043169	molecular_function	cation binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 4001

Chain	Residue
A	ASN100
A	ARG158
A	ASP167
A	HIS201
A	HOH4014
A	HOH4094
A	HOH4125

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 4002

Chain	Residue
A	ARG337
A	ARG195
A	ASN298

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 4003

Chain	Residue
B	ASN100
B	ARG158
B	ASP167
B	HIS201
B	HOH4012
B	HOH4030
B	HOH4307

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 4004

Chain	Residue
B	ARG195
B	ASN298
B	ARG337

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA C 4005

Chain	Residue
C	ASN100
C	ARG158
C	ASP167
C	HIS201
C	HOH4022
C	HOH4047
C	HOH4060

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 4006

Chain	Residue
C	ARG195
C	ASN298
C	ARG337

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA D 4007

Chain	Residue
D	ASN100
D	ARG158
D	ASP167
D	HIS201
D	HOH4016
D	HOH4038
D	HOH4041

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 4008

Chain	Residue
D	ARG195
D	ASN298
D	ARG337

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8193143","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8681972","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8994970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11412124","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11960990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7897663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8757803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9385631","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"UniProtKB","id":"P04746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP300
A	ASP197
A	GLU233

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
B	ASP236
B	ASP197

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
C	ASP236
C	ASP197

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
D	ASP236
D	ASP197

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

Chain	Residue	Details
B	ASP300
B	ASP197
B	GLU233

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

Chain	Residue	Details
C	ASP300
C	ASP197
C	GLU233

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
D	ASP300
D	ASP197
D	GLU233

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
A	ASP197
A	GLU233

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
B	ASP197
B	GLU233

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
C	ASP197
C	GLU233

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
D	ASP197
D	GLU233

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1amy

Chain	Residue	Details
A	ASP236
A	ASP197

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)