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5EVC

Crystal structure of putative aspartate racemase from Salmonella Typhimurium complexed with sulfate and potassium

Functional Information from GO Data
ChainGOidnamespacecontents
A0006520biological_processamino acid metabolic process
A0006807biological_processobsolete nitrogen compound metabolic process
A0016597molecular_functionamino acid binding
A0016743molecular_functioncarboxyl- or carbamoyltransferase activity
A0016853molecular_functionisomerase activity
A0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
A0036361molecular_functionracemase activity, acting on amino acids and derivatives
A0046872molecular_functionmetal ion binding
A0047661molecular_functionamino-acid racemase activity
B0006520biological_processamino acid metabolic process
B0006807biological_processobsolete nitrogen compound metabolic process
B0016597molecular_functionamino acid binding
B0016743molecular_functioncarboxyl- or carbamoyltransferase activity
B0016853molecular_functionisomerase activity
B0016855molecular_functionracemase and epimerase activity, acting on amino acids and derivatives
B0036361molecular_functionracemase activity, acting on amino acids and derivatives
B0046872molecular_functionmetal ion binding
B0047661molecular_functionamino-acid racemase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue K A 301
ChainResidue
AMET11
ATHR194
AGLU195
ASO4302
AHOH421

site_idAC2
Number of Residues10
Detailsbinding site for residue SO4 A 302
ChainResidue
ATHR124
ALYS163
AK301
AHOH413
AHOH417
AHOH482
AMET11
AARG49
ACYS83
ATHR85

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 303
ChainResidue
AVAL24
AGLU25
AARG27
AHOH480
AHOH523

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 304
ChainResidue
AASP111
AARG220
AHOH441
AHOH451
BHIS28
BALA29
BSER30
BGLN34

site_idAC5
Number of Residues5
Detailsbinding site for residue FMT A 305
ChainResidue
APRO113
ASER115
AARG164
AHOH401
BCYS31

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 306
ChainResidue
ASER59
ATYR61
AARG62
BHIS118

site_idAC7
Number of Residues5
Detailsbinding site for residue K B 301
ChainResidue
BMET11
BTHR194
BGLU195
BSO4302
BF303

site_idAC8
Number of Residues10
Detailsbinding site for residue SO4 B 302
ChainResidue
BMET11
BARG49
BCYS83
BTHR85
BTHR124
BLYS163
BK301
BHOH402
BHOH406
BHOH486

site_idAC9
Number of Residues6
Detailsbinding site for residue F B 303
ChainResidue
BCYS83
BASN84
BCYS193
BTHR194
BK301
BHOH402

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL B 304
ChainResidue
AARG224
BARG27
BGLN34
BTHR232
BHOH434

site_idAD2
Number of Residues5
Detailsbinding site for residue K B 305
ChainResidue
BVAL24
BGLU25
BARG27
BHOH461
BHOH515

Functional Information from PROSITE/UniProt
site_idPS00923
Number of Residues9
DetailsASP_GLU_RACEMASE_1 Aspartate and glutamate racemases signature 1. VIpC.NTAHY
ChainResidueDetails
AVAL80-TYR88

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. IImGCTEIPlI
ChainResidueDetails
AILE189-ILE199

222036

PDB entries from 2024-07-03

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