1Z5U

Crystal structure of S. typhimurium AphA complexed with cyclic-AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003993	molecular_function	acid phosphatase activity
A	0016787	molecular_function	hydrolase activity
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0003993	molecular_function	acid phosphatase activity
B	0016787	molecular_function	hydrolase activity
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding
C	0003993	molecular_function	acid phosphatase activity
C	0016787	molecular_function	hydrolase activity
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
D	0003993	molecular_function	acid phosphatase activity
D	0016787	molecular_function	hydrolase activity
D	0030288	cellular_component	outer membrane-bounded periplasmic space
D	0042597	cellular_component	periplasmic space
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASP46
A	ASP48
A	ASP169
A	HOH504
A	HOH505
A	HOH613

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 503

Chain	Residue
B	HOH509
B	HOH619
B	HOH620
B	ASP46
B	ASP48
B	ASP169

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 505

Chain	Residue
C	ASP46
C	ASP48
C	ASP169
C	HOH227
C	HOH470
C	HOH471

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 507

Chain	Residue
D	ASP46
D	ASP48
D	ASP169
D	HOH338
D	HOH473
D	HOH474

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CMP A 502

Chain	Residue
A	ASP48
A	PHE58
A	ASP70
A	TYR72
A	LEU73
A	GLY115
A	ARG116
A	THR194
A	TYR195
A	HOH503
A	HOH505
A	HOH613
A	HOH614

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CMP B 504

Chain	Residue
B	ASP48
B	PHE58
B	TYR72
B	GLY115
B	ARG116
B	THR194
B	TYR195
B	HOH511
B	HOH512
B	HOH620
B	HOH621
B	HOH622

---

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CMP C 506

Chain	Residue
C	ASP48
C	PHE58
C	TYR72
C	GLY115
C	ARG116
C	THR194
C	TYR195
C	HOH230
C	HOH231
C	HOH471
C	HOH472

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE CMP D 508

Chain	Residue
D	ASP46
D	ASP48
D	PHE58
D	TYR72
D	LEU73
D	GLY115
D	ARG116
D	LYS154
D	THR194
D	TYR195
D	HOH339
D	HOH340
D	HOH430
D	HOH473
D	HOH475
D	HOH476

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:17570338

Chain	Residue	Details
A	ASP46
B	ASP46
C	ASP46
D	ASP46

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:17570338

Chain	Residue	Details
A	ASP48
B	ASP48
C	ASP48
D	ASP48

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:17570338

Chain	Residue	Details
A	ASP46
B	ASP169
C	ASP46
C	ASP48
C	THR114
C	LYS154
C	ASP169
D	ASP46
D	ASP48
D	THR114
D	LYS154
A	ASP48
D	ASP169
A	THR114
A	LYS154
A	ASP169
B	ASP46
B	ASP48
B	THR114
B	LYS154

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1q91

Chain	Residue	Details
A	ASP48
A	ASP46

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1q91

Chain	Residue	Details
B	ASP48
B	ASP46

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1q91

Chain	Residue	Details
C	ASP48
C	ASP46

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1q91

Chain	Residue	Details
D	ASP48
D	ASP46

---