5VVW

Structure of MurC from Pseudomonas aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
A	0009058	biological_process	biosynthetic process
A	0016881	molecular_function	acid-amino acid ligase activity
B	0005524	molecular_function	ATP binding
B	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
B	0009058	biological_process	biosynthetic process
B	0016881	molecular_function	acid-amino acid ligase activity
C	0005524	molecular_function	ATP binding
C	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
C	0009058	biological_process	biosynthetic process
C	0016881	molecular_function	acid-amino acid ligase activity
D	0005524	molecular_function	ATP binding
D	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
D	0009058	biological_process	biosynthetic process
D	0016881	molecular_function	acid-amino acid ligase activity
E	0005524	molecular_function	ATP binding
E	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
E	0009058	biological_process	biosynthetic process
E	0016881	molecular_function	acid-amino acid ligase activity
F	0005524	molecular_function	ATP binding
F	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
F	0009058	biological_process	biosynthetic process
F	0016881	molecular_function	acid-amino acid ligase activity
G	0005524	molecular_function	ATP binding
G	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
G	0009058	biological_process	biosynthetic process
G	0016881	molecular_function	acid-amino acid ligase activity
H	0005524	molecular_function	ATP binding
H	0008763	molecular_function	UDP-N-acetylmuramate-L-alanine ligase activity
H	0009058	biological_process	biosynthetic process
H	0016881	molecular_function	acid-amino acid ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO A 401

Chain	Residue
A	ARG233
A	ASP251
C	ARG233

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO B 401

Chain	Residue
B	ALA26
B	GLY30
B	ARG151
B	LEU152

---

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO C 401

Chain	Residue
C	GLY30
C	LEU152
C	LEU161
C	ALA26
C	GLY27

---

site_id	AC4
Number of Residues	9
Details	binding site for residue EDO G 401

Chain	Residue
D	VAL227
D	ASP228
D	ASP229
D	PRO230
D	ARG233
G	VAL227
G	ASP228
G	PRO230
G	ARG233

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO G 402

Chain	Residue
G	ALA252
G	ASP253
G	ARG255
G	ARG272

---

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO G 403

Chain	Residue
G	VAL254
G	PRO273
G	THR301
G	ASP302
G	HOH535

---

site_id	AC7
Number of Residues	5
Details	binding site for residue EDO H 401

Chain	Residue
H	ALA26
H	GLY27
H	GLY30
H	ARG151
H	LEU152

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00046

Chain	Residue	Details
A	GLY122
B	GLY122
C	GLY122
D	GLY122
E	GLY122
F	GLY122
G	GLY122
H	GLY122

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