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3ZVI

Methylaspartate ammonia lyase from Clostridium tetanomorphum mutant L384A

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 Residues4
DetailsBINDING SITE FOR RESIDUE ROP A 1420
ChainResidue
AGLN73
ACYS361
AHOH2123
AHOH2124

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1421
ChainResidue
AHOH2297
AASP238
AGLU273
AASP307
AHOH2261
AHOH2296

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ROP B 1420
ChainResidue
BGLN73
BTHR360
BCYS361
BHOH2087
BHOH2088

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 1421
ChainResidue
BASP238
BGLU273
BASP307
BHOH2214
BHOH2253
BHOH2254

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1416
ChainResidue
AGLU401
AARG404
ALEU408
AHOH2205
AHOH2383
AHOH2413
BVAL64

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1416
ChainResidue
AHOH2114
BGLU401
BARG404
BLEU408
BHOH2162
BHOH2358
BHOH2381

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1417
ChainResidue
ALYS399
AASN403
BPRO10
BLEU12
BLYS49
BHOH2011
BHOH2382
BHOH2383

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1418
ChainResidue
BGLY79
BARG80
BASP81
BTHR128
BASP334

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1419
ChainResidue
BARG177
BTYR178
BLYS203
BLYS210
BTYR214
BHOH2233

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1422
ChainResidue
ALYS2
BASP176
BTYR178
BASP179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:11748244, ECO:0000269|PubMed:19670200
ChainResidueDetails
ALYS331
BLYS331

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLN172
ATHR360
BGLN172
BTHR360

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11748244, ECO:0000269|PubMed:22614383
ChainResidueDetails
AASP307
BASP238
BGLU273
BASP307
AASP238
AGLU273

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BGLN329
BCYS361
AGLN329
ACYS361

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AHIS194
BHIS194

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 468
ChainResidueDetails
AGLN172electrostatic stabiliser
AHIS194electrostatic stabiliser
AASP238metal ligand
AGLU273metal ligand
AASP307metal ligand
AGLN329electrostatic stabiliser
ALYS331electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA2
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

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PDB entries from 2024-05-15

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