Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PLG

Crystal structure of human PHGDH complexed with Compound 15

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0051287	molecular_function	NAD binding
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0051287	molecular_function	NAD binding
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0051287	molecular_function	NAD binding
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0051287	molecular_function	NAD binding
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0051287	molecular_function	NAD binding
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0051287	molecular_function	NAD binding
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0051287	molecular_function	NAD binding
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue ONS A 401

Chain	Residue
A	GLY154
A	THR207
A	LEU210
A	ARG236
C	THR89
C	VAL95
A	ARG155
A	ILE156
A	TYR174
A	ASP175
A	PRO176
A	ILE177
A	ILE178
A	HIS206

site_id	AC2
Number of Residues	14
Details	binding site for residue ONS B 401

Chain	Residue
B	GLY154
B	ARG155
B	ILE156
B	TYR174
B	ASP175
B	PRO176
B	ILE178
B	HIS206
B	THR207
B	PRO208
B	LEU210
B	THR213
D	THR89
D	VAL95

site_id	AC3
Number of Residues	13
Details	binding site for residue ONS C 401

Chain	Residue
C	GLY152
C	ARG155
C	ILE156
C	TYR174
C	ASP175
C	PRO176
C	ILE178
C	HIS206
C	THR207
C	LEU210
C	THR213
C	LEU216
C	ARG236

site_id	AC4
Number of Residues	14
Details	binding site for residue ONS D 401

Chain	Residue
D	GLY154
D	ARG155
D	ILE156
D	TYR174
D	ASP175
D	PRO176
D	ILE177
D	ILE178
D	HIS206
D	THR207
D	LEU210
D	THR213
D	LEU216
D	ARG236

site_id	AC5
Number of Residues	13
Details	binding site for residue ONS E 401

Chain	Residue
E	GLY154
E	ARG155
E	ILE156
E	TYR174
E	ASP175
E	PRO176
E	ILE177
E	HIS206
E	THR207
E	SER212
E	THR213
E	LEU216
E	ARG236

site_id	AC6
Number of Residues	10
Details	binding site for residue MLT E 402

Chain	Residue
A	ARG135
E	ARG54
E	SER55
E	ARG75
E	ALA76
E	GLY77
E	THR78
E	HIS283
E	ALA286
E	GLN292

site_id	AC7
Number of Residues	14
Details	binding site for residue ONS F 401

Chain	Residue
F	LEU151
F	GLY152
F	GLY154
F	ARG155
F	ILE156
F	TYR174
F	ASP175
F	PRO176
F	ILE177
F	HIS206
F	THR207
F	PRO208
F	LEU216
F	ARG236

site_id	AC8
Number of Residues	7
Details	binding site for residue MLT F 402

Chain	Residue
F	SER55
F	ARG75
F	ALA76
F	GLY77
F	THR78
F	HIS283
F	ALA286

site_id	AC9
Number of Residues	13
Details	binding site for residue ONS G 401

Chain	Residue
G	GLY154
G	ARG155
G	ILE156
G	TYR174
G	ASP175
G	PRO176
G	ILE177
G	HIS206
G	THR207
G	PRO208
G	LEU210
G	THR213
G	LEU216

site_id	AD1
Number of Residues	9
Details	binding site for residue MLT G 402

Chain	Residue
C	ARG135
G	ARG54
G	SER55
G	ARG75
G	ALA76
G	GLY77
G	ASN102
G	ARG236
G	HIS283

site_id	AD2
Number of Residues	14
Details	binding site for residue ONS H 401

Chain	Residue
H	GLY154
H	ARG155
H	ILE156
H	TYR174
H	ASP175
H	PRO176
H	ILE177
H	HIS206
H	THR207
H	PRO208
H	LEU210
H	SER212
H	THR213
H	LEU216

site_id	AD3
Number of Residues	11
Details	binding site for residue MLT H 402

Chain	Residue
D	ARG135
H	ARG54
H	SER55
H	ARG75
H	GLY77
H	THR78
H	ASN102
H	ARG236
H	HIS283
H	ALA286
H	GLN292

Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	28
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGILGlGRIGrevatrmqsfgmk.TIgYD

Chain	Residue	Details
A	LEU148-ASP175

site_id	PS00670
Number of Residues	23
Details	D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. IWplCDFItVHtPllpsTtgLlN

Chain	Residue	Details
A	ILE196-ASN218

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. CKkGvRVVNcARGgIVD

Chain	Residue	Details
A	CYS225-ASP241

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE:

Chain	Residue	Details
A	ARG236
B	ARG236
C	ARG236
D	ARG236
E	ARG236
F	ARG236
G	ARG236
H	ARG236

site_id	SWS_FT_FI2
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
C	GLU265
D	GLU265
E	GLU265
F	GLU265
G	GLU265
H	GLU265
A	GLU265
B	GLU265

site_id	SWS_FT_FI3
Number of Residues	8
Details	ACT_SITE: Proton donor

Chain	Residue	Details
B	HIS283
C	HIS283
F	HIS283
G	HIS283
H	HIS283
A	HIS283
D	HIS283
E	HIS283

site_id	SWS_FT_FI4
Number of Residues	56
Details	BINDING: BINDING => ECO:0000269\|Ref.21

Chain	Residue	Details
B	ARG155
B	ASP175
B	THR207
B	CYS234
B	ASP260
B	HIS283
C	THR78
C	ARG155
C	ASP175
C	THR207
C	CYS234
C	ASP260
C	HIS283
D	THR78
D	ARG155
D	ASP175
D	THR207
D	CYS234
D	ASP260
D	HIS283
E	THR78
E	ARG155
E	ASP175
E	THR207
E	CYS234
E	ASP260
E	HIS283
F	THR78
F	ARG155
F	ASP175
F	THR207
F	CYS234
F	ASP260
F	HIS283
G	THR78
G	ARG155
G	ASP175
G	THR207
G	CYS234
G	ASP260
G	HIS283
H	THR78
H	ARG155
H	ASP175
H	THR207
H	CYS234
H	ASP260
H	HIS283
A	ARG155
A	ASP175
A	THR207
A	CYS234
A	ASP260
A	HIS283
B	THR78
A	THR78

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER14
B	SER14
C	SER14
D	SER14
E	SER14
F	SER14
G	SER14
H	SER14

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:Q61753

Chain	Residue	Details
B	LYS21
F	LYS21
G	LYS21
H	LYS21
A	LYS21
C	LYS21
D	LYS21
E	LYS21

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:Q61753

Chain	Residue	Details
B	LYS58
F	LYS58
G	LYS58
H	LYS58
A	LYS58
C	LYS58
D	LYS58
E	LYS58

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	THR78
F	THR78
G	THR78
H	THR78
A	THR78
C	THR78
D	THR78
E	THR78

site_id	SWS_FT_FI9
Number of Residues	16
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:25114211

Chain	Residue	Details
E	LYS21
F	LYS21
G	LYS21
H	LYS21
D	LYS21
A	LYS21
B	LYS21
C	LYS21

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