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

3ZVH

Methylaspartate ammonia lyase from Clostridium tetanomorphum mutant Q73A

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0019553biological_processglutamate catabolic process via L-citramalate
A0031419molecular_functioncobalamin binding
A0046872molecular_functionmetal ion binding
A0050096molecular_functionmethylaspartate ammonia-lyase activity
B0016829molecular_functionlyase activity
B0019553biological_processglutamate catabolic process via L-citramalate
B0031419molecular_functioncobalamin binding
B0046872molecular_functionmetal ion binding
B0050096molecular_functionmethylaspartate ammonia-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1421
ChainResidue
AASP238
AGLU273
AASP307
AHOH2180
AHOH2181
AHOH2182

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1421
ChainResidue
BHOH2182
BHOH2183
BHOH2184
BASP238
BGLU273
BASP307

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1416
ChainResidue
AGLU401
AARG404
ALEU408
AHOH2127

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1416
ChainResidue
AHOH2060
BGLU401
BARG404
BLEU408
BHOH2116
BHOH2256

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1417
ChainResidue
APRO10
AGLY11
ALYS49
AGLU51
AHOH2261
BASN403

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 1417
ChainResidue
BASN199
BGLU201
BGLU202

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1418
ChainResidue
AGLU308
ATRP309
AASN311

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1418
ChainResidue
ALYS2
BASP176
BTYR178
BASP179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11748244, ECO:0000269|PubMed:19670200
ChainResidueDetails
BLYS331

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BGLN172
BTHR360

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11748244, ECO:0000269|PubMed:22614383
ChainResidueDetails
BASP238
BGLU273
BASP307

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
BGLN329
BOCS361

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
BHIS194

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 468
ChainResidueDetails
BGLN172electrostatic stabiliser
BHIS194electrostatic stabiliser
BASP238metal ligand
BGLU273metal ligand
BASP307metal ligand
BGLN329electrostatic stabiliser
BLYS331electrostatic stabiliser, proton acceptor, proton donor

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon