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3OCF

Crystal structure of fumarate lyase:delta crystallin from Brucella melitensis in native form

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006099biological_processtricarboxylic acid cycle
A0008797molecular_functionaspartate ammonia-lyase activity
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0008797molecular_functionaspartate ammonia-lyase activity
B0016829molecular_functionlyase activity
C0003824molecular_functioncatalytic activity
C0006099biological_processtricarboxylic acid cycle
C0008797molecular_functionaspartate ammonia-lyase activity
C0016829molecular_functionlyase activity
D0003824molecular_functioncatalytic activity
D0006099biological_processtricarboxylic acid cycle
D0008797molecular_functionaspartate ammonia-lyase activity
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 458
ChainResidue
CILE41
CPRO42
CALA43

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL D 458
ChainResidue
DILE41
DPRO42
DALA43
DARG373

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 458
ChainResidue
BALA43
BARG373
BILE41
BPRO42

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 458
ChainResidue
AILE41
APRO42
AALA43
AARG373
AHOH581

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 459
ChainResidue
DGLY10
DGLU11
DHOH540
DHOH557

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO D 460
ChainResidue
BGLN338
BEDO459
DASN342
DTYR366
DASN367
DSER370

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 459
ChainResidue
BASN342
BTYR366
BASN367
BSER370
DGLN338
DEDO460

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 459
ChainResidue
AGLN338
AASN342
ATYR366
AASN367
ASER370
AEDO460
CGLN338

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 460
ChainResidue
AGLN338
AEDO459
CASN342
CTYR366
CASN367
CSER370

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY316-ASN325

222415

PDB entries from 2024-07-10

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