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2GB3

Crystal structure of Aspartate aminotransferase (tm1698) from Thermotoga maritima at 2.50 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
C0003824molecular_functioncatalytic activity
C0006520biological_processamino acid metabolic process
C0008483molecular_functiontransaminase activity
C0009058biological_processbiosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
D0003824molecular_functioncatalytic activity
D0006520biological_processamino acid metabolic process
D0008483molecular_functiontransaminase activity
D0009058biological_processbiosynthetic process
D0030170molecular_functionpyridoxal phosphate binding
E0003824molecular_functioncatalytic activity
E0006520biological_processamino acid metabolic process
E0008483molecular_functiontransaminase activity
E0009058biological_processbiosynthetic process
E0030170molecular_functionpyridoxal phosphate binding
F0003824molecular_functioncatalytic activity
F0006520biological_processamino acid metabolic process
F0008483molecular_functiontransaminase activity
F0009058biological_processbiosynthetic process
F0030170molecular_functionpyridoxal phosphate binding
Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SVSKkfSAcGARVG
ChainResidueDetails
ASER229-GLY242

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP201
ATYR124
BALA67

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
DHIS65

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
EHIS65

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
FHIS65

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AALA67
BASP201
BTYR124

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
DALA67
CASP201
CTYR124

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
CALA67
DASP201
DTYR124

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
FALA67
EASP201
ETYR124

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
FASP201
FTYR124
EALA67

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AHIS65

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BHIS65

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
CHIS65

224201

PDB entries from 2024-08-28

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