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

1ASN

CRYSTAL STRUCTURES OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE IN TWO CONFORMATIONS: COMPARISON OF AN UNLIGANDED OPEN AND TWO LIGANDED CLOSED FORMS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0004838molecular_functionL-tyrosine:2-oxoglutarate aminotransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0009094biological_processL-phenylalanine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0033585biological_processL-phenylalanine biosynthetic process from chorismate via phenylpyruvate
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0004838molecular_functionL-tyrosine:2-oxoglutarate aminotransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0009094biological_processL-phenylalanine biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0033585biological_processL-phenylalanine biosynthetic process from chorismate via phenylpyruvate
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 410
ChainResidue
AGLY38
ATRP140
AASN194
APHE360
AARG386
AHOH517
AHOH528
AILE17

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 410
ChainResidue
BILE17
BGLY38
BTRP140
BASN194
BARG386

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 411
ChainResidue
AGLY107
AGLY108
ATHR109
AASN194
AASP222
AALA224
ATYR225
ASER255
ASER257
ALYS258
AARG266
AHOH421
AHOH508
AHOH528
BTYR70

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 411
ChainResidue
ATYR70
BGLY107
BGLY108
BTHR109
BTRP140
BASN194
BASP222
BALA224
BTYR225
BSER255
BSER257
BLYS258
BARG266

site_idACA
Number of Residues4
Details
ChainResidue
ALYS258
APLP411
BARG292
AARG386

site_idACB
Number of Residues4
Details
ChainResidue
BLYS258
BPLP411
AARG292
BARG386

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SYSKnfGLyNERVG
ChainResidueDetails
ASER255-GLY268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
ChainResidueDetails
AGLY38
BGLY38

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
ChainResidueDetails
ATRP140
BTRP140

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
ChainResidueDetails
AASN194
BASN194

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC
ChainResidueDetails
AARG386
BARG386

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11148029, ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240, ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW, ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF, ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY, ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS, ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB, ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE, ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG, ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN, ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC, ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V, ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W, ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6, ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8, ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS, ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO, ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61, ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y, ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ, ECO:0007744|PDB:5EAA
ChainResidueDetails
ALYS258
BLYS258

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATRP140
AASP222
ALYS258

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTRP140
BASP222
BLYS258

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AILE73

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BILE73

site_idMCSA1
Number of Residues3
DetailsM-CSA 777
ChainResidueDetails
ATRP140steric role
AASP222proton shuttle (general acid/base)
ALYS258proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 777
ChainResidueDetails
BTRP140steric role
BASP222proton shuttle (general acid/base)
BLYS258proton shuttle (general acid/base)

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon