6GS2

Crystal Structure of the GatD/MurT Enzyme Complex from Staphylococcus aureus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004359	molecular_function	glutaminase activity
A	0006541	biological_process	glutamine metabolic process
A	0008360	biological_process	regulation of cell shape
A	0009236	biological_process	cobalamin biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0016874	molecular_function	ligase activity
A	0071555	biological_process	cell wall organization
A	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
B	0005524	molecular_function	ATP binding
B	0008270	molecular_function	zinc ion binding
B	0008360	biological_process	regulation of cell shape
B	0009058	biological_process	biosynthetic process
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016874	molecular_function	ligase activity
B	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
B	0016881	molecular_function	acid-amino acid ligase activity
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization
B	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
C	0003824	molecular_function	catalytic activity
C	0004359	molecular_function	glutaminase activity
C	0006541	biological_process	glutamine metabolic process
C	0008360	biological_process	regulation of cell shape
C	0009236	biological_process	cobalamin biosynthetic process
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0016874	molecular_function	ligase activity
C	0071555	biological_process	cell wall organization
C	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
D	0005524	molecular_function	ATP binding
D	0008270	molecular_function	zinc ion binding
D	0008360	biological_process	regulation of cell shape
D	0009058	biological_process	biosynthetic process
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016874	molecular_function	ligase activity
D	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
D	0016881	molecular_function	acid-amino acid ligase activity
D	0046872	molecular_function	metal ion binding
D	0071555	biological_process	cell wall organization
D	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue 144 A 301

Chain	Residue
A	ASP138
A	HOH468
A	HOH492
C	ASP138
C	THR139
C	THR159
A	THR139
A	GLY158
A	THR159
A	HIS179
A	HOH409
A	HOH410
A	HOH421
A	HOH443

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site_id	AC2
Number of Residues	4
Details	binding site for residue PEG A 302

Chain	Residue
A	ILE213
A	PRO214
B	SER239
B	ASP241

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site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 501

Chain	Residue
B	CYS202
B	CYS205
B	CYS224
B	CYS226

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site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 502

Chain	Residue
B	HIS189
B	ASP262
B	HOH610
B	HOH634
B	HOH689

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN D 501

Chain	Residue
D	CYS202
D	CYS205
D	CYS224
D	CYS226

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000305|PubMed:30154570

Chain	Residue	Details
B	ASP349
D	ASP349

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:30154570

Chain	Residue	Details
B	CYS202
B	CYS205
B	CYS224
B	CYS226
D	CYS202
D	CYS205
D	CYS224
D	CYS226

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H2WZ38, ECO:0000255|HAMAP-Rule:MF_02213

Chain	Residue	Details
A	ARG128
C	ARG128

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