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1KD0

Crystal Structure of beta-methylaspartase from Clostridium tetanomorphum. Apo-structure.

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 Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
AGLU401
AARG404
AHOH719
AHOH737
AHOH992

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 702
ChainResidue
BGLU401
BARG404
BHOH727
BHOH749

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
AGLN329
BGLN329
BCYS361
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 2024-06-12

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