1QD6

OUTER MEMBRANE PHOSPHOLIPASE A FROM ESCHERICHIA COLI

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0004620	molecular_function	phospholipase activity
C	0006629	biological_process	lipid metabolic process
C	0016020	cellular_component	membrane
D	0004620	molecular_function	phospholipase activity
D	0006629	biological_process	lipid metabolic process
D	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 1

Chain	Residue
C	ARG147
C	SER152
C	HOH285
C	HOH294
D	SER106
D	HOH275

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 2

Chain	Residue
D	HOH302
C	SER106
D	ARG147
D	SER152

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HDS C 270

Chain	Residue
C	TYR92
C	TYR114
C	HIS142
C	SER144
C	ASN145
C	GLY146
C	HOH285
D	TYR39
D	PHE69
D	TRP98
D	PHE109
D	VAL263
D	LEU265
D	HOH275

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HDS D 270

Chain	Residue
C	TYR39
C	LEU71
C	TRP98
C	PHE109
C	VAL263
C	LEU265
D	TYR92
D	HIS142
D	SER144
D	ASN145
D	GLY146
D	HOH302

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	266
Details	TRANSMEM: Beta stranded

Chain	Residue	Details
C	TYR33-THR45
C	ASP65-ARG79
C	SER86-TRP98
C	PHE109-PHE128
C	TRP131-SER144
C	SER154-ASN166
C	TRP169-VAL178
C	LEU197-LEU203
C	ALA206-TYR214
C	GLY222-PRO230
C	ARG236-TYR245
C	ASN255-ASN266
D	TYR33-THR45
D	ASP65-ARG79
D	SER86-TRP98
D	PHE109-PHE128
D	TRP131-SER144
D	SER154-ASN166
D	TRP169-VAL178
D	LEU197-LEU203
D	ALA206-TYR214
D	GLY222-PRO230
D	ARG236-TYR245
D	ASN255-ASN266

---

site_id	SWS_FT_FI2
Number of Residues	132
Details	TOPO_DOM: Extracellular

Chain	Residue	Details
C	SER46-LYS64
C	GLN99-PRO108
C	ASN145-ARG153
C	VAL179-GLN196
C	ASN215-GLY221
C	GLY246-PHE254
D	SER46-LYS64
D	GLN99-PRO108
D	ASN145-ARG153
D	VAL179-GLN196
D	ASN215-GLY221
D	GLY246-PHE254

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	TOPO_DOM: Periplasmic

Chain	Residue	Details
C	GLY80-ASN85
C	ALA129-GLY130
C	GLY167-ASN168
C	GLY204-ASP205
C	ILE231-VAL235
C	ASP267-PHE269
D	GLY80-ASN85
D	ALA129-GLY130
D	GLY167-ASN168
D	GLY204-ASP205
D	ILE231-VAL235
D	ASP267-PHE269

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305

Chain	Residue	Details
C	HIS142
D	HIS142

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:2040286

Chain	Residue	Details
C	SER144
D	SER144

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: in dimeric form

Chain	Residue	Details
C	SER106
C	SER152
D	SER106
D	ARG147
D	SER152
C	ARG147

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: in monomeric form

Chain	Residue	Details
C	ASP184
D	ASP184

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 650

Chain	Residue	Details
C	SER106	metal ligand
C	HIS142	proton acceptor, proton donor
C	SER144	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
C	GLY146	electrostatic stabiliser
C	ARG147	metal ligand
C	SER152	metal ligand
C	ASN156	electrostatic stabiliser, increase basicity

---

site_id	MCSA2
Number of Residues	7
Details	M-CSA 650

Chain	Residue	Details
D	SER106	metal ligand
D	HIS142	proton acceptor, proton donor
D	SER144	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
D	GLY146	electrostatic stabiliser
D	ARG147	metal ligand
D	SER152	metal ligand
D	ASN156	electrostatic stabiliser, increase basicity

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