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1KXV

Camelid VHH Domains in Complex with Porcine Pancreatic alpha-Amylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005975biological_processcarbohydrate metabolic process
A0016052biological_processcarbohydrate catabolic process
A0016160molecular_functionamylase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031404molecular_functionchloride ion binding
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004556molecular_functionalpha-amylase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005975biological_processcarbohydrate metabolic process
B0016052biological_processcarbohydrate catabolic process
B0016160molecular_functionamylase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031404molecular_functionchloride ion binding
B0043169molecular_functioncation binding
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP212
BASP212

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
APHE248
BPHE248

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8193143, ECO:0000269|PubMed:8681972, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:8994970, ECO:0000269|PubMed:9385631
ChainResidueDetails
ACYS115
AASP173
ATYR182
AASN216
BCYS115
BASP173
BTYR182
BASN216

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11412124, ECO:0000269|PubMed:11960990, ECO:0000269|PubMed:7897663, ECO:0000269|PubMed:8757803, ECO:0000269|PubMed:9385631
ChainResidueDetails
AVAL210
AGLU352
BVAL210
BGLU352

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALEU313
BLEU313

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746
ChainResidueDetails
APHE315
BPHE315

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P04746
ChainResidueDetails
ALEU16
BLEU16

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AILE427
BILE427

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP300
AASP197
AGLU233

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP300
BASP197
BGLU233

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP197
AGLU233

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP197
BGLU233

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AASP197

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP236
BASP197

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PDB entries from 2024-11-06

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