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12AS

ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004071molecular_functionaspartate-ammonia ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006529biological_processasparagine biosynthetic process
A0006974biological_processDNA damage response
A0016874molecular_functionligase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0070981biological_processL-asparagine biosynthetic process
B0004071molecular_functionaspartate-ammonia ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006529biological_processasparagine biosynthetic process
B0006974biological_processDNA damage response
B0016874molecular_functionligase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0070981biological_processL-asparagine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ASN A 331
ChainResidue
ASER251
AARG255
AGLY293
AGLY294
AAMP332
AHOH371
AASP46
ASER72
AALA74
ALYS77
AGLN116
AASP118
ATYR218

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ASN B 331
ChainResidue
BASP46
BSER72
BALA74
BLYS77
BGLN116
BASP118
BTYR218
BASP219
BSER251
BARG255
BGLY292
BGLY293
BAMP332

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP A 332
ChainResidue
AARG100
AGLU103
ALEU109
AHIS110
ASER111
AVAL114
AGLN116
AGLU248
ALEU249
ASER250
ASER251
AGLY294
AGLY296
AARG299
AILE310
AASN331
AHOH386

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AMP B 332
ChainResidue
BARG100
BGLU103
BLEU109
BHIS110
BSER111
BVAL114
BGLN116
BGLU248
BLEU249
BSER250
BSER251
BGLY296
BARG299
BASN331
BHOH385

site_idNU1
Number of Residues1
DetailsAMP BINDING (CATALYTIC) SITE (CHAIN A).
ChainResidue
AAMP332

site_idNU2
Number of Residues1
DetailsAMP BINDING (CATALYTIC) SITE (CHAIN B).
ChainResidue
BAMP332

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 9437423
ChainResidueDetails
AASP46
AGLN116
AARG100

site_idMCSA1
Number of Residues6
DetailsM-CSA 75
ChainResidueDetails
AASP46hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG100electrostatic stabiliser, hydrogen bond donor
AGLN116electrostatic stabiliser, hydrogen bond donor
AASP235metal ligand
AGLU248metal ligand
ASER251electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 75
ChainResidueDetails
BASP46hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG100electrostatic stabiliser, hydrogen bond donor
BGLN116electrostatic stabiliser, hydrogen bond donor
BASP235metal ligand
BGLU248metal ligand
BSER251electrostatic stabiliser

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PDB entries from 2024-09-18

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