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3CBF

Crystal structure of LysN, alpha-aminoadipate aminotransferase, from Thermus thermophilus HB27

Functional Information from GO Data
ChainGOidnamespacecontents
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0019878biological_processlysine biosynthetic process via aminoadipic acid
A0030170molecular_functionpyridoxal phosphate binding
A0047536molecular_function2-aminoadipate transaminase activity
A1901605biological_processalpha-amino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0019878biological_processlysine biosynthetic process via aminoadipic acid
B0030170molecular_functionpyridoxal phosphate binding
B0047536molecular_function2-aminoadipate transaminase activity
B1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE N5F A 500
ChainResidue
AILE22
AASP202
ATYR205
ASER235
ASER237
ALYS238
AARG245
AARG368
BTYR70
AARG23
AGLY39
AGLY40
AGLY99
ASER100
AGLN101
ATYR125
AASN174

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE N5F B 501
ChainResidue
ATYR70
BILE22
BARG23
BGLY39
BGLY40
BGLY99
BSER100
BGLN101
BTYR125
BASN174
BASP202
BTYR205
BSER235
BSER237
BLYS238
BARG245
BARG368

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18831049, ECO:0000269|PubMed:19632206
ChainResidueDetails
AGLY40
AASN174
AARG368
BGLY40
BASN174
BARG368

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.5
ChainResidueDetails
ATYR70
AARG245
BTYR70
BARG245

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ASER100
AASP202
ASER235
BSER100
BASP202
BSER235

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Recognizes the side-chain carboxyl group of acidic compounds
ChainResidueDetails
AARG23
BARG23

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS263
BLYS263

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS238
ATYR125
AASP202

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BLYS238
BTYR125
BASP202

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR125
AASP202

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BTYR125
BASP202

221716

PDB entries from 2024-06-26

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