1W2I

Crystal structuore of acylphosphatase from Pyrococcus horikoshii complexed with formate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003998	molecular_function	acylphosphatase activity
A	0016787	molecular_function	hydrolase activity
B	0003998	molecular_function	acylphosphatase activity
B	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A1092

Chain	Residue
A	GLY18
A	PHE19
A	ARG20
A	TRP21
A	HOH2022
A	HOH2026

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT A1093

Chain	Residue
B	GLY18
B	TRP21
B	SER22
A	ARG20
A	GLN80
A	HOH2107

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT B1092

Chain	Residue
B	GLY18
B	PHE19
B	ARG20
B	TRP21
B	HOH2021
B	HOH2025

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT B1093

Chain	Residue
B	ARG88

---

Functional Information from PROSITE/UniProt

site_id	PS00150
Number of Residues	11
Details	ACYLPHOSPHATASE_1 Acylphosphatase signature 1. IyGrVQGVgFR

Chain	Residue	Details
A	ILE10-ARG20

---

site_id	PS00151
Number of Residues	17
Details	ACYLPHOSPHATASE_2 Acylphosphatase signature 2. GWVRNlpdGsVeavleG

Chain	Residue	Details
A	GLY34-GLY50

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	172
Details	Domain: {"description":"Acylphosphatase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"PubMed","id":"15779887","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASN38
A	ARG20

---

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

Chain	Residue	Details
B	ASN38
B	ARG20

---