Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1NM9

Crystal structure of recombinant human salivary amylase mutant W58A

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
A0009311biological_processoligosaccharide metabolic process
A0016160molecular_functionamylase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031404molecular_functionchloride ion binding
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP197

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU233

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12527308, ECO:0000269|PubMed:15299664, ECO:0007744|PDB:1SMD
ChainResidueDetails
AASN100
AARG158
AASP167
AARG195
AHIS201
AASN298
AARG337

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P04746
ChainResidueDetails
AASP300

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000250|UniProtKB:P00687
ChainResidueDetails
APCA1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:1710976
ChainResidueDetails
AASN350
AASN459

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Deamidated asparagine; partial; alternate => ECO:0000269|PubMed:1710976
ChainResidueDetails
AASN412

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:1710976
ChainResidueDetails
AASN412

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN461

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

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP197
AGLU233

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP236
AASP197

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon