Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6DHL

Bovine glutamate dehydrogenase complexed with epicatechin-3-gallate (ECG)

Replaces: 3QMUReplaces: 3MVQ

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006520	biological_process	amino acid metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
B	0006520	biological_process	amino acid metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
C	0006520	biological_process	amino acid metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
D	0006520	biological_process	amino acid metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
E	0006520	biological_process	amino acid metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
F	0006520	biological_process	amino acid metabolic process
F	0016491	molecular_function	oxidoreductase activity
F	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
G	0006520	biological_process	amino acid metabolic process
G	0016491	molecular_function	oxidoreductase activity
G	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
H	0006520	biological_process	amino acid metabolic process
H	0016491	molecular_function	oxidoreductase activity
H	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
I	0006520	biological_process	amino acid metabolic process
I	0016491	molecular_function	oxidoreductase activity
I	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
J	0006520	biological_process	amino acid metabolic process
J	0016491	molecular_function	oxidoreductase activity
J	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
K	0006520	biological_process	amino acid metabolic process
K	0016491	molecular_function	oxidoreductase activity
K	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
L	0006520	biological_process	amino acid metabolic process
L	0016491	molecular_function	oxidoreductase activity
L	0016639	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue XEG A 601

Chain	Residue
A	HIS85
F	HIS209
F	LYS387
F	SER393
F	ARG396
A	ARG86
A	CYS115
A	ALA116
A	ASP119
A	VAL120
A	ARG459
A	LYS488
A	ARG491

site_id	AC2
Number of Residues	13
Details	binding site for residue XEG B 601

Chain	Residue
A	ILE203
A	HIS209
A	LYS387
A	SER393
A	ARG396
B	ARG86
B	CYS115
B	ALA116
B	ASP119
B	VAL120
B	ARG459
B	LYS488
B	ARG491

site_id	AC3
Number of Residues	13
Details	binding site for residue XEG C 601

Chain	Residue
C	HIS85
C	ARG86
C	CYS115
C	ALA116
C	ASP119
C	VAL120
C	ARG459
C	LYS488
C	ARG491
C	VAL492
D	LYS387
D	SER393
D	ARG396

site_id	AC4
Number of Residues	14
Details	binding site for residue XEG D 601

Chain	Residue
D	HIS85
D	ARG86
D	CYS115
D	ALA116
D	ASP119
D	VAL120
D	ARG459
D	LYS488
D	ARG491
E	ILE203
E	HIS209
E	LYS387
E	SER393
E	ARG396

site_id	AC5
Number of Residues	13
Details	binding site for residue XEG E 601

Chain	Residue
C	HIS209
C	LYS387
C	SER393
C	ARG396
E	HIS85
E	ARG86
E	CYS115
E	ALA116
E	ASP119
E	VAL120
E	ARG459
E	LYS488
E	ARG491

site_id	AC6
Number of Residues	13
Details	binding site for residue XEG F 601

Chain	Residue
B	HIS209
B	SER393
B	ARG396
F	HIS85
F	ARG86
F	CYS115
F	ALA116
F	ASP119
F	VAL120
F	ARG459
F	LYS488
F	ARG491
F	VAL492

site_id	AC7
Number of Residues	11
Details	binding site for residue XEG G 601

Chain	Residue
G	HIS85
G	ARG86
G	CYS115
G	ALA116
G	ASP119
G	VAL120
G	ARG459
G	LYS488
L	LYS387
L	SER393
L	ARG396

site_id	AC8
Number of Residues	13
Details	binding site for residue XEG H 601

Chain	Residue
H	ASP119
H	VAL120
H	ARG459
H	LYS488
G	ILE203
G	HIS209
G	LYS387
G	SER393
G	ARG396
H	HIS85
H	ARG86
H	CYS115
H	ALA116

site_id	AC9
Number of Residues	12
Details	binding site for residue XEG I 601

Chain	Residue
I	HIS85
I	ARG86
I	CYS115
I	ALA116
I	ASP119
I	VAL120
I	ARG459
I	LYS488
I	ARG491
J	LYS387
J	SER393
J	ARG396

site_id	AD1
Number of Residues	14
Details	binding site for residue XEG J 601

Chain	Residue
J	HIS85
J	ARG86
J	CYS115
J	ALA116
J	ASP119
J	VAL120
J	ARG459
J	LYS488
J	ARG491
K	ILE203
K	HIS209
K	LYS387
K	SER393
K	ARG396

site_id	AD2
Number of Residues	12
Details	binding site for residue XEG K 601

Chain	Residue
I	HIS209
I	LYS387
I	SER393
I	ARG396
K	ARG86
K	CYS115
K	ALA116
K	ASP119
K	VAL120
K	ARG459
K	LYS488
K	ARG491

site_id	AD3
Number of Residues	12
Details	binding site for residue XEG L 601

Chain	Residue
H	ILE203
H	HIS209
H	LYS387
H	SER393
H	ARG396
L	HIS85
L	ARG86
L	CYS115
L	VAL120
L	ARG459
L	LYS488
L	ARG491

Functional Information from PROSITE/UniProt

site_id	PS00074
Number of Residues	14
Details	GLFV_DEHYDROGENASE Glu / Leu / Phe / Val dehydrogenases active site. VpfGGAKaGvkiNP

Chain	Residue	Details
A	VAL120-PRO133

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	144
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11254391","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12653548","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10011","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	24
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	108
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	36
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22076378","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	12
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	48
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	12
Details	Modified residue: {"description":"ADP-ribosylcysteine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	96
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26443","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	24
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	12
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P10860","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	12
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00367","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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