Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CN1

2.75 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Pseudomonas putida in Complex with Uridine-diphosphate-2(n-acetylglucosaminyl) butyric acid, (2R)-2-(phosphonooxy)propanoic acid and Magnesium

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0008360	biological_process	regulation of cell shape
A	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
A	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization
B	0003824	molecular_function	catalytic activity
B	0005737	cellular_component	cytoplasm
B	0008360	biological_process	regulation of cell shape
B	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
B	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
B	0051301	biological_process	cell division
B	0071555	biological_process	cell wall organization
C	0003824	molecular_function	catalytic activity
C	0005737	cellular_component	cytoplasm
C	0008360	biological_process	regulation of cell shape
C	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
C	0051301	biological_process	cell division
C	0071555	biological_process	cell wall organization
D	0003824	molecular_function	catalytic activity
D	0005737	cellular_component	cytoplasm
D	0008360	biological_process	regulation of cell shape
D	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
D	0051301	biological_process	cell division
D	0071555	biological_process	cell wall organization
E	0003824	molecular_function	catalytic activity
E	0005737	cellular_component	cytoplasm
E	0008360	biological_process	regulation of cell shape
E	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
E	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
E	0051301	biological_process	cell division
E	0071555	biological_process	cell wall organization
F	0003824	molecular_function	catalytic activity
F	0005737	cellular_component	cytoplasm
F	0008360	biological_process	regulation of cell shape
F	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
F	0009252	biological_process	peptidoglycan biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
F	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
F	0051301	biological_process	cell division
F	0071555	biological_process	cell wall organization
G	0003824	molecular_function	catalytic activity
G	0005737	cellular_component	cytoplasm
G	0008360	biological_process	regulation of cell shape
G	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
G	0009252	biological_process	peptidoglycan biosynthetic process
G	0016740	molecular_function	transferase activity
G	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
G	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
G	0051301	biological_process	cell division
G	0071555	biological_process	cell wall organization
H	0003824	molecular_function	catalytic activity
H	0005737	cellular_component	cytoplasm
H	0008360	biological_process	regulation of cell shape
H	0008760	molecular_function	UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
H	0009252	biological_process	peptidoglycan biosynthetic process
H	0016740	molecular_function	transferase activity
H	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
H	0019277	biological_process	UDP-N-acetylgalactosamine biosynthetic process
H	0051301	biological_process	cell division
H	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue EPU A 501

Chain	Residue
A	LYS22
A	VAL164
A	SER165
A	VAL166
A	THR167
A	THR307
A	ASP308
A	ILE330
A	PHE331
A	LEU373
A	HOH601
A	ASN23
A	HOH605
A	ALA94
A	SER121
A	ARG122
A	PRO123
A	VAL124
A	ASP125
A	LEU126

site_id	AC2
Number of Residues	9
Details	binding site for residue 0V5 A 502

Chain	Residue
A	ARG93
A	CYS117
A	ALA118
A	ILE119
A	ARG400
A	MG503
A	HOH602
A	HOH606
A	HOH607

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 503

Chain	Residue
A	0V5502
A	HOH602
A	HOH607
A	HOH636
A	HOH639

site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 504

Chain	Residue
A	GLU263
A	HOH638

site_id	AC5
Number of Residues	18
Details	binding site for residue EPU B 500

Chain	Residue
B	LYS22
B	ASN23
B	ALA94
B	SER121
B	ARG122
B	PRO123
B	VAL124
B	ASP125
B	LEU126
B	THR163
B	SER165
B	VAL166
B	THR167
B	ASP308
B	ILE330
B	PHE331
B	LEU373
B	HOH601

site_id	AC6
Number of Residues	6
Details	binding site for residue MG B 502

Chain	Residue
B	ARG400
B	0V5501
B	HOH609
B	HOH615
B	HOH630
B	HOH632

site_id	AC7
Number of Residues	19
Details	binding site for residue EPU C 501

Chain	Residue
C	LYS22
C	ASN23
C	ALA94
C	SER121
C	ARG122
C	PRO123
C	VAL124
C	ASP125
C	LEU126
C	THR163
C	SER165
C	VAL166
C	THR167
C	THR307
C	ASP308
C	ILE330
C	PHE331
C	LEU373
C	HOH603

site_id	AC8
Number of Residues	5
Details	binding site for residue MG C 503

Chain	Residue
C	0V5502
C	HOH601
C	HOH619
C	HOH624
C	HOH643

site_id	AC9
Number of Residues	2
Details	binding site for residue CL C 504

Chain	Residue
C	SER121
C	GLU332

site_id	AD1
Number of Residues	20
Details	binding site for residue EPU D 500

Chain	Residue
D	THR307
D	ASP308
D	ILE330
D	PHE331
D	LEU373
D	HOH615
D	HOH629
D	LYS22
D	ASN23
D	SER121
D	ARG122
D	PRO123
D	VAL124
D	ASP125
D	LEU126
D	THR163
D	VAL164
D	SER165
D	VAL166
D	THR167

site_id	AD2
Number of Residues	6
Details	binding site for residue MG D 502

Chain	Residue
D	ARG400
D	0V5501
D	HOH601
D	HOH627
D	HOH631
D	HOH635

site_id	AD3
Number of Residues	18
Details	binding site for residue EPU E 500

Chain	Residue
E	LYS22
E	ASN23
E	ALA94
E	SER121
E	ARG122
E	PRO123
E	VAL124
E	ASP125
E	LEU126
E	HIS127
E	THR163
E	SER165
E	VAL166
E	THR167
E	ASP308
E	ILE330
E	PHE331
E	LEU373

site_id	AD4
Number of Residues	5
Details	binding site for residue MG E 502

Chain	Residue
E	0V5501
E	HOH602
E	HOH608
E	HOH627
E	HOH631

site_id	AD5
Number of Residues	18
Details	binding site for residue EPU F 501

Chain	Residue
F	LYS22
F	ASN23
F	ALA94
F	SER121
F	ARG122
F	PRO123
F	VAL124
F	ASP125
F	LEU126
F	THR163
F	SER165
F	VAL166
F	THR167
F	THR307
F	ASP308
F	ILE330
F	PHE331
F	HOH617

site_id	AD6
Number of Residues	6
Details	binding site for residue MG F 503

Chain	Residue
F	ARG400
F	0V5502
F	HOH601
F	HOH602
F	HOH622
F	HOH628

site_id	AD7
Number of Residues	3
Details	binding site for residue CL F 504

Chain	Residue
F	GLN410
F	ARG417
F	ARG418

site_id	AD8
Number of Residues	20
Details	binding site for residue EPU G 500

Chain	Residue
G	LYS22
G	ASN23
G	ALA94
G	SER121
G	ARG122
G	PRO123
G	VAL124
G	ASP125
G	LEU126
G	VAL164
G	SER165
G	VAL166
G	THR167
G	THR307
G	ASP308
G	ILE330
G	PHE331
G	LEU373
G	HOH603
G	HOH610

site_id	AD9
Number of Residues	5
Details	binding site for residue MG G 502

Chain	Residue
G	0V5501
G	HOH601
G	HOH611
G	HOH613
G	HOH617

site_id	AE1
Number of Residues	19
Details	binding site for residue EPU H 501

Chain	Residue
H	LYS22
H	ASN23
H	SER121
H	ARG122
H	PRO123
H	VAL124
H	ASP125
H	LEU126
H	THR163
H	SER165
H	VAL166
H	THR167
H	THR307
H	ASP308
H	ILE330
H	PHE331
H	LEU373
H	HOH601
H	HOH627

site_id	AE2
Number of Residues	6
Details	binding site for residue MG H 503

Chain	Residue
H	ARG400
H	0V5502
H	HOH604
H	HOH614
H	HOH624
H	HOH641

site_id	AE3
Number of Residues	1
Details	binding site for residue CL H 504

Chain	Residue
H	ARG77

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	64
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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