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1U08

Crystal Structure and Reactivity of YbdL from Escherichia coli Identify a Methionine Aminotransferase Function.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0010326molecular_functionmethionine-oxo-acid transaminase activity
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0010326molecular_functionmethionine-oxo-acid transaminase activity
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 400
ChainResidue
AGLY99
ASER233
ALYS236
ALYS244
AHOH448
BTYR63
AALA100
ATHR101
ATYR125
AASN170
AASN174
AASP202
AVAL204
ATYR205

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 1400
ChainResidue
ATYR63
BGLY99
BALA100
BTHR101
BTYR125
BASN170
BASN174
BASP202
BTYR205
BSER233
BLYS236
BLYS244
BHOH1435

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS236
BLYS236

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS236
ATYR125
AASP202

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS236
BTYR205

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
APRO65

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BPRO65

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS236
BTYR125
BASP202

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR125
AASP202
BTHR67

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATHR67
BTYR125
BASP202

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS236
ATYR86
AASP202

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS236
BTYR86
BASP202

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS236
ATYR128
AASP202

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS236
BTYR128
BASP202

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS236
ATYR205

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PDB entries from 2024-11-13

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