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3PM6

Crystal structure of a putative fructose-1,6-biphosphate aldolase from Coccidioides immitis solved by combined SAD MR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004332molecular_functionfructose-bisphosphate aldolase activity
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016832molecular_functionaldehyde-lyase activity
A0046872molecular_functionmetal ion binding
B0004332molecular_functionfructose-bisphosphate aldolase activity
B0005975biological_processcarbohydrate metabolic process
B0006096biological_processglycolytic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016832molecular_functionaldehyde-lyase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 304
ChainResidue
BTHR20

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 306
ChainResidue
BTRP57
BHOH339

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 307
ChainResidue
BGLN89

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 308
ChainResidue
BARG96

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 309
ChainResidue
BLYS95
BHOH357

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 303
ChainResidue
AGLN89

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 304
ChainResidue
AILE93

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 305
ChainResidue
AARG96

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 306
ChainResidue
ALYS95
AGLU131
AIOD307

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 307
ChainResidue
AGLU131
AIOD306

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 309
ChainResidue
AARG239

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 310
ChainResidue
ATYR204

site_idBC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 311
ChainResidue
ATYR195

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 314
ChainResidue
ALYS261

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 315
ChainResidue
AHIS21

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 316
ChainResidue
AHOH458

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 311
ChainResidue
BASN252
BHOH370

site_idBC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 313
ChainResidue
AASN194

site_idCC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 314
ChainResidue
BHIS21

site_idCC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 315
ChainResidue
BHOH398

site_idCC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 318
ChainResidue
AGLU164

site_idCC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 318
ChainResidue
BILE93

site_idCC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD B 319
ChainResidue
BLYS95
BHOH394

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 319
ChainResidue
AHIS87
AHIS192
AHIS223

site_idCC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 320
ChainResidue
BHIS87
BHIS223
BHOH400
BHOH402
BHOH403

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP86
BASP86

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS87
BASP116
BGLU146
BHIS192
BGLY193
BHIS223
BGLY224
BASN245
AASP116
AGLU146
AHIS192
AGLY193
AHIS223
AGLY224
AASN245
BHIS87

225681

PDB entries from 2024-10-02

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