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4PG5

Crystal structure of S. aureus Homoserine Dehydrogenase at pH6.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004412molecular_functionhomoserine dehydrogenase activity
A0006520biological_processamino acid metabolic process
A0009086biological_processmethionine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050661molecular_functionNADP binding
B0004412molecular_functionhomoserine dehydrogenase activity
B0006520biological_processamino acid metabolic process
B0009086biological_processmethionine biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue ACT A 501
ChainResidue
AVAL79
AMET80
AGLY81
AALA103
AASN104
ALYS105

site_idAC2
Number of Residues5
Detailsbinding site for residue ACT A 502
ChainResidue
AARG386
AHOH661
ALEU242
ATYR244
AASP269

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 503
ChainResidue
AGLN216
AVAL217
AGLY257
AVAL259

site_idAC4
Number of Residues1
Detailsbinding site for residue ACT A 504
ChainResidue
AGLU264

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 505
ChainResidue
ATHR170
AASN237
AASP240

site_idAC6
Number of Residues4
Detailsbinding site for residue ACT A 506
ChainResidue
ATYR281
ATYR297
AHOH682
BTYR285

site_idAC7
Number of Residues4
Detailsbinding site for residue ACT A 507
ChainResidue
AHIS363
ALYS365
AGLY414
AHOH607

site_idAC8
Number of Residues3
Detailsbinding site for residue GOL A 508
ChainResidue
AASP240
BASP46
BSER48

site_idAC9
Number of Residues3
Detailsbinding site for residue PEG A 509
ChainResidue
AASN221
AVAL223
AARG225

site_idAD1
Number of Residues6
Detailsbinding site for residue ACT B 501
ChainResidue
BGLN216
BVAL217
BILE218
BGLY257
BLYS258
BVAL259

site_idAD2
Number of Residues3
Detailsbinding site for residue ACT B 502
ChainResidue
BLYS224
BARG226
BGLU264

site_idAD3
Number of Residues5
Detailsbinding site for residue ACT B 503
ChainResidue
BTYR244
BARG386
BVAL398
BDMS510
BHOH619

site_idAD4
Number of Residues5
Detailsbinding site for residue ACT B 504
ChainResidue
BLEU108
BLYS219
BLEU220
BHOH603
BHOH604

site_idAD5
Number of Residues7
Detailsbinding site for residue DMS B 505
ChainResidue
AHIS413
AGLY414
AHOH672
BLYS376
BALA377
BLEU379
BPHE381

site_idAD6
Number of Residues6
Detailsbinding site for residue DMS B 506
ChainResidue
BVAL79
BMET80
BGLY81
BALA103
BASN104
BLYS105

site_idAD7
Number of Residues3
Detailsbinding site for residue DMS B 507
ChainResidue
BHIS413
BGLY414
BTYR415

site_idAD8
Number of Residues5
Detailsbinding site for residue GOL B 508
ChainResidue
BVAL38
BILE39
BGLN57
BTYR58
BHOH635

site_idAD9
Number of Residues4
Detailsbinding site for residue PEG B 509
ChainResidue
BGLY230
BTHR232
BASP418
BLYS419

site_idAE1
Number of Residues4
Detailsbinding site for residue DMS B 510
ChainResidue
BLEU242
BASP269
BARG386
BACT503

Functional Information from PROSITE/UniProt
site_idPS01042
Number of Residues23
DetailsHOMOSER_DHGENASE Homoserine dehydrogenase signature. AkrlGFAea.DPtdDVeGvDaarK
ChainResidueDetails
AALA183-LYS205

222415

PDB entries from 2024-07-10

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