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2O0R

The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009016molecular_functionsuccinyldiaminopimelate transaminase activity
A0009058biological_processbiosynthetic process
A0009085biological_processlysine biosynthetic process
A0009089biological_processlysine biosynthetic process via diaminopimelate
A0009274cellular_componentpeptidoglycan-based cell wall
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0030170molecular_functionpyridoxal phosphate binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009016molecular_functionsuccinyldiaminopimelate transaminase activity
B0009058biological_processbiosynthetic process
B0009085biological_processlysine biosynthetic process
B0009089biological_processlysine biosynthetic process via diaminopimelate
B0009274cellular_componentpeptidoglycan-based cell wall
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
AARG76
ATHR179
AHOH788

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 602
ChainResidue
BALA178
BTHR179
BHOH711

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 603
ChainResidue
BHOH931
BHOH932
BALA191
BHOH929
BHOH930

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
ATHR12
APHE14
AASP120
BTYR263
BHOH745

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
ATYR260
ATYR263
AHOH714
BTHR12
BPHE14
BTYR119
BASP120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY109
AASP218
BGLY109
BASP218

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALLP232
BLLP232

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP207
ATYR119

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR122
BASP198

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BPRO61

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP207
BTYR119

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APRO61

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP198
ATYR119

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP198
BTYR119

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APHE118
AASP198

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BPHE118
BASP198

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR122
AASP198

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PDB entries from 2024-10-09

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