Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZZ7

Crystal structure of methylmalonate-semialdehyde dehydrogenase (DddC) from Oceanimonas doudoroffii

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
A	0006210	biological_process	thymine catabolic process
A	0006574	biological_process	L-valine catabolic process
A	0016491	molecular_function	oxidoreductase activity
B	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
B	0006210	biological_process	thymine catabolic process
B	0006574	biological_process	L-valine catabolic process
B	0016491	molecular_function	oxidoreductase activity
C	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
C	0006210	biological_process	thymine catabolic process
C	0006574	biological_process	L-valine catabolic process
C	0016491	molecular_function	oxidoreductase activity
D	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
D	0006210	biological_process	thymine catabolic process
D	0006574	biological_process	L-valine catabolic process
D	0016491	molecular_function	oxidoreductase activity
E	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
E	0006210	biological_process	thymine catabolic process
E	0006574	biological_process	L-valine catabolic process
E	0016491	molecular_function	oxidoreductase activity
F	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
F	0006210	biological_process	thymine catabolic process
F	0006574	biological_process	L-valine catabolic process
F	0016491	molecular_function	oxidoreductase activity
G	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
G	0006210	biological_process	thymine catabolic process
G	0006574	biological_process	L-valine catabolic process
G	0016491	molecular_function	oxidoreductase activity
H	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
H	0006210	biological_process	thymine catabolic process
H	0006574	biological_process	L-valine catabolic process
H	0016491	molecular_function	oxidoreductase activity
I	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
I	0006210	biological_process	thymine catabolic process
I	0006574	biological_process	L-valine catabolic process
I	0016491	molecular_function	oxidoreductase activity
J	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
J	0006210	biological_process	thymine catabolic process
J	0006574	biological_process	L-valine catabolic process
J	0016491	molecular_function	oxidoreductase activity
K	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
K	0006210	biological_process	thymine catabolic process
K	0006574	biological_process	L-valine catabolic process
K	0016491	molecular_function	oxidoreductase activity
L	0004491	molecular_function	methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity
L	0006210	biological_process	thymine catabolic process
L	0006574	biological_process	L-valine catabolic process
L	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	binding site for residue NAD A 501

Chain	Residue
A	THR146
A	LYS205
A	VAL208
A	PHE222
A	VAL223
A	GLY224
A	SER225
A	ILE228
A	LEU246
A	GLY247
A	GLY248
A	PRO147
A	CYS280
A	GLU382
A	PHE384
A	ASN410
A	PHE449
A	PHE148
A	ASN149
A	LYS172
A	PRO173
A	SER174
A	GLU175
A	ARG176

site_id	AC2
Number of Residues	21
Details	binding site for residue NAD C 501

Chain	Residue
C	THR146
C	PRO147
C	PHE148
C	ASN149
C	LYS172
C	GLU175
C	ARG176
C	LYS205
C	PHE222
C	VAL223
C	GLY224
C	SER225
C	ILE228
C	LEU246
C	GLY247
C	GLY248
C	CYS280
C	GLU382
C	PHE384
C	ASN410
C	PHE449

site_id	AC3
Number of Residues	21
Details	binding site for residue NAD D 501

Chain	Residue
D	THR146
D	PRO147
D	PHE148
D	ASN149
D	LYS172
D	GLU175
D	ARG176
D	LYS205
D	PHE222
D	VAL223
D	GLY224
D	SER225
D	ILE228
D	LEU246
D	GLY247
D	GLY248
D	CYS280
D	GLU382
D	PHE384
D	ASN410
D	PHE449

site_id	AC4
Number of Residues	25
Details	binding site for residue NAD E 501

Chain	Residue
E	ILE145
E	THR146
E	PRO147
E	PHE148
E	ASN149
E	LYS172
E	SER174
E	GLU175
E	ARG176
E	LYS205
E	VAL208
E	PHE222
E	VAL223
E	GLY224
E	SER225
E	ILE228
E	LEU246
E	GLY247
E	GLY248
E	CYS280
E	GLU382
E	PHE384
E	ASN410
E	PHE449
E	HOH608

site_id	AC5
Number of Residues	26
Details	binding site for residue NAD I 501

Chain	Residue
I	GLU175
I	ARG176
I	LYS205
I	VAL208
I	PHE222
I	VAL223
I	GLY224
I	SER225
I	ILE228
I	LEU246
I	GLY247
I	GLY248
I	CYS280
I	GLU382
I	PHE384
I	ASN410
I	PHE449
I	HOH639
I	ILE145
I	THR146
I	PRO147
I	PHE148
I	ASN149
I	LYS172
I	PRO173
I	SER174

site_id	AC6
Number of Residues	25
Details	binding site for residue NAD L 501

Chain	Residue
L	ILE145
L	THR146
L	PRO147
L	PHE148
L	ASN149
L	LYS172
L	PRO173
L	GLU175
L	ARG176
L	LYS205
L	VAL208
L	PHE222
L	VAL223
L	GLY224
L	SER225
L	ILE228
L	LEU246
L	GLY247
L	GLY248
L	CYS280
L	GLU382
L	PHE384
L	ASN410
L	PHE449
L	HOH606

Functional Information from PROSITE/UniProt

site_id	PS00070
Number of Residues	12
Details	ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgSSGERCMALS

Chain	Residue	Details
A	PHE273-SER284

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