Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2ZP7

Crystal structure of LysN, alpha-aminoadipate aminotransferase (Leucine complex), from Thermus thermophilus HB27

Replaces: 2ZG5Replaces: 2DTV

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008483	molecular_function	transaminase activity
A	0009058	biological_process	biosynthetic process
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
A	0030170	molecular_function	pyridoxal phosphate binding
A	0047536	molecular_function	2-aminoadipate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009058	biological_process	biosynthetic process
B	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
B	0030170	molecular_function	pyridoxal phosphate binding
B	0047536	molecular_function	2-aminoadipate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009058	biological_process	biosynthetic process
C	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
C	0030170	molecular_function	pyridoxal phosphate binding
C	0047536	molecular_function	2-aminoadipate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009058	biological_process	biosynthetic process
D	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
D	0030170	molecular_function	pyridoxal phosphate binding
D	0047536	molecular_function	2-aminoadipate transaminase activity
E	0008483	molecular_function	transaminase activity
E	0009058	biological_process	biosynthetic process
E	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
E	0030170	molecular_function	pyridoxal phosphate binding
E	0047536	molecular_function	2-aminoadipate transaminase activity
F	0008483	molecular_function	transaminase activity
F	0009058	biological_process	biosynthetic process
F	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
F	0030170	molecular_function	pyridoxal phosphate binding
F	0047536	molecular_function	2-aminoadipate transaminase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP A 600

Chain	Residue
A	GLY99
A	SER237
A	LYS238
A	ARG245
A	LEU700
C	TYR70
A	SER100
A	GLN101
A	TYR125
A	ILE169
A	ASN174
A	ASP202
A	TYR205
A	SER235

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LEU A 700

Chain	Residue
A	GLY39
A	GLY40
A	ASN174
A	LYS238
A	ARG368
C	TYR70

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP B 600

Chain	Residue
B	GLY99
B	SER100
B	GLN101
B	TYR125
B	ILE169
B	ASN174
B	ASP202
B	TYR205
B	SER235
B	SER237
B	LYS238
B	ARG245
B	LEU700
D	TYR70

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LEU B 700

Chain	Residue
B	GLY39
B	GLY40
B	ASN174
B	LYS238
B	ARG368
D	TYR70

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP C 600

Chain	Residue
A	TYR70
C	GLY99
C	SER100
C	GLN101
C	TYR125
C	ILE169
C	ASN174
C	ASP202
C	TYR205
C	SER235
C	SER237
C	LYS238
C	ARG245

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP D 600

Chain	Residue
B	TYR70
D	GLY99
D	SER100
D	GLN101
D	TYR125
D	ILE169
D	ASN174
D	ASP202
D	TYR205
D	SER235
D	SER237
D	LYS238
D	ARG245

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PLP E 600

Chain	Residue
E	GLY99
E	SER100
E	GLN101
E	TYR125
E	ILE169
E	ASN174
E	ASP202
E	TYR205
E	SER235
E	SER237
E	LYS238
E	ARG245
E	LEU700
F	TYR70

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LEU E 700

Chain	Residue
E	GLY40
E	TYR125
E	ASN174
E	LYS238
E	ARG368

site_id	AC9
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLP F 600

Chain	Residue
E	TYR70
E	LEU268
F	GLY99
F	SER100
F	GLN101
F	TYR125
F	ASN174
F	ASP202
F	TYR205
F	SER235
F	SER237
F	LYS238
F	ARG245

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:18831049, ECO:0000269\|PubMed:19632206

Chain	Residue	Details
A	GLY40
D	GLY40
D	ASN174
D	ARG368
E	GLY40
E	ASN174
E	ARG368
F	GLY40
F	ASN174
F	ARG368
A	ASN174
A	ARG368
B	GLY40
B	ASN174
B	ARG368
C	GLY40
C	ASN174
C	ARG368

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|Ref.5

Chain	Residue	Details
A	TYR70
E	ARG245
F	TYR70
F	ARG245
A	ARG245
B	TYR70
B	ARG245
C	TYR70
C	ARG245
D	TYR70
D	ARG245
E	TYR70

site_id	SWS_FT_FI3
Number of Residues	18
Details	BINDING:

Chain	Residue	Details
A	SER100
D	SER100
D	ASP202
D	SER235
E	SER100
E	ASP202
E	SER235
F	SER100
F	ASP202
F	SER235
A	ASP202
A	SER235
B	SER100
B	ASP202
B	SER235
C	SER100
C	ASP202
C	SER235

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Recognizes the side-chain carboxyl group of acidic compounds

Chain	Residue	Details
A	ARG23
B	ARG23
C	ARG23
D	ARG23
E	ARG23
F	ARG23

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250

Chain	Residue	Details
A	LYS263
B	LYS263
C	LYS263
D	LYS263
E	LYS263
F	LYS263

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	LYS238
A	TYR125
A	ASP202

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	TYR125
D	ASP202

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
E	TYR125
E	ASP202

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
F	TYR125
F	ASP202

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	LYS238
B	TYR125
B	ASP202

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	LYS238
C	TYR125
C	ASP202

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
D	LYS238
D	TYR125
D	ASP202

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
E	LYS238
E	TYR125
E	ASP202

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
F	LYS238
F	TYR125
F	ASP202

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
A	TYR125
A	ASP202

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
B	TYR125
B	ASP202

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ay4

Chain	Residue	Details
C	TYR125
C	ASP202

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)