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3VOS

Crystal structure of Aspartate semialdehyde dehydrogenase Complexed With glycerol and sulfate From Mycobacterium tuberculosis H37Rv

Replaces:  3LLGReplaces:  3KUB
Functional Information from GO Data
ChainGOidnamespacecontents
A0004073molecular_functionaspartate-semialdehyde dehydrogenase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0009085biological_processlysine biosynthetic process
A0009086biological_processmethionine biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009097biological_processisoleucine biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0019877biological_processdiaminopimelate biosynthetic process
A0046983molecular_functionprotein dimerization activity
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0071266biological_process'de novo' L-methionine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
ACYS130
AGLN157
AGLY161
AGLU224
AARG249
AHIS256
ASO4404
AHOH825
AHOH850

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AGLY188
AGLY189
ALEU191
APHE193
AHOH613
AHOH621
AHOH680
AHOH685
AHOH722
AHOH835

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 403
ChainResidue
AARG229
APHE230
AARG233
AHOH682
AHOH849

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
AARG99
AASN129
ACYS130
ALYS227
AGOL401
AHOH786
AHOH851
AHOH909

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
AGLU271
AARG274
AHOH842

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 406
ChainResidue
AHIS118
AARG120
AHOH933

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 407
ChainResidue
AARG233
AHOH662
AHOH930

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 408
ChainResidue
AARG43
AGLU53
AGLY73
ASER74
AHOH862
AHOH869
AHOH871
AHOH898

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 409
ChainResidue
AGLY12
AGLN13
AVAL14
AARG43
AGLY163
ALEU164
AHOH629
AHOH823
AHOH876
AHOH910

Functional Information from PROSITE/UniProt
site_idPS01103
Number of Residues15
DetailsASD Aspartate-semialdehyde dehydrogenase signature. VSgtCvRVpvftGHS
ChainResidueDetails
AVAL243-SER257

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305|PubMed:22683789
ChainResidueDetails
ACYS130

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AHIS256

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG39
AARG99
AGLN157
ASER160
ALYS227
AARG249
AASN325
ATHR11

219869

PDB entries from 2024-05-15

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