2D0Q

Complex of Fe-type NHase with Cyclohexyl isocyanide, photo-activated for 1hr at 277K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016829	molecular_function	lyase activity
A	0018822	molecular_function	nitrile hydratase activity
A	0046872	molecular_function	metal ion binding
A	0046914	molecular_function	transition metal ion binding
B	0016829	molecular_function	lyase activity
B	0018822	molecular_function	nitrile hydratase activity
B	0046914	molecular_function	transition metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 300

Chain	Residue
A	CYS109
A	CSD112
A	SER113
A	CYS114
A	CYI1301

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1410

Chain	Residue
B	HOH1811
A	HOH1613
A	HOH1771
A	HOH1799
B	HOH1780

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1438

Chain	Residue
A	HOH1585
A	HOH1656
A	HOH1664
A	HOH1694
B	HOH1673
B	HOH1741

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1439

Chain	Residue
A	HOH1616
B	HOH1790
B	HOH1904
B	HOH1924
B	HOH1925
B	HOH1927

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 1612

Chain	Residue
B	HOH1716
B	HOH1755
B	HOH1802
B	HOH1827

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1517

Chain	Residue
A	GLU139
A	HOH1754
B	HOH1750
B	HOH1769
B	HOH1866

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1560

Chain	Residue
A	ASP37
A	HOH1665
A	HOH1725
A	HOH1735
A	HOH1747

---

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CYI A 1301

Chain	Residue
A	GLN90
A	CSD112
A	SER113
A	CYS114
A	TRP117
A	FE300
B	VAL52
B	ARG56
B	TYR72
B	TYR76

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18948265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26333053","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16636455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17716629","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20221653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26333053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Photo-activation state of Fe-type NHase in anaerobic and aerobic conditions.","authors":["Kawano Y.","Hashimoto K.","Odaka M.","Nakayama H.","Takio K.","Endo I.","Kamiya N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2014","submissionDatabase":"PDB data bank","title":"Reaction intermediate of nitrile hydratase determined by time-resolved crystallography reveals the cysteine-sulfenic acid ligand to be a catalytic nucleophile.","authors":["Yamanaka Y.","Hashimoto K.","Noguchi K.","Yohda M.","Odaka M."]}},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CYZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X20","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X24","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X25","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X26","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X28","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16636455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17716629","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20221653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26333053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Photo-activation state of Fe-type NHase in anaerobic and aerobic conditions.","authors":["Kawano Y.","Hashimoto K.","Odaka M.","Nakayama H.","Takio K.","Endo I.","Kamiya N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2014","submissionDatabase":"PDB data bank","title":"Reaction intermediate of nitrile hydratase determined by time-resolved crystallography reveals the cysteine-sulfenic acid ligand to be a catalytic nucleophile.","authors":["Yamanaka Y.","Hashimoto K.","Noguchi K.","Yohda M.","Odaka M."]}},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CYZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X20","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X24","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X25","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X26","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X28","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16636455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17716629","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20221653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26333053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Photo-activation state of Fe-type NHase in anaerobic and aerobic conditions.","authors":["Kawano Y.","Hashimoto K.","Odaka M.","Nakayama H.","Takio K.","Endo I.","Kamiya N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2014","submissionDatabase":"PDB data bank","title":"Reaction intermediate of nitrile hydratase determined by time-resolved crystallography reveals the cysteine-sulfenic acid ligand to be a catalytic nucleophile.","authors":["Yamanaka Y.","Hashimoto K.","Noguchi K.","Yohda M.","Odaka M."]}},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CYZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X20","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X24","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X25","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X26","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X28","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"16636455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17716629","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20221653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26333053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Photo-activation state of Fe-type NHase in anaerobic and aerobic conditions.","authors":["Kawano Y.","Hashimoto K.","Odaka M.","Nakayama H.","Takio K.","Endo I.","Kamiya N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2014","submissionDatabase":"PDB data bank","title":"Reaction intermediate of nitrile hydratase determined by time-resolved crystallography reveals the cysteine-sulfenic acid ligand to be a catalytic nucleophile.","authors":["Yamanaka Y.","Hashimoto K.","Noguchi K.","Yohda M.","Odaka M."]}},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CYZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2D0Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2QDY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZCF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X20","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X24","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X25","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X26","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X28","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"16636455","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17716629","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948265","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20221653","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26333053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Photo-activation state of Fe-type NHase in anaerobic and aerobic conditions.","authors":["Kawano Y.","Hashimoto K.","Odaka M.","Nakayama H.","Takio K.","Endo I.","Kamiya N."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2014","submissionDatabase":"PDB data bank","title":"Reaction intermediate of nitrile hydratase determined by time-resolved crystallography reveals the cysteine-sulfenic acid ligand to be a catalytic nucleophile.","authors":["Yamanaka Y.","Hashimoto K.","Noguchi K.","Yohda M.","Odaka M."]}},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CYZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CZ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZCF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3A8O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X20","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X24","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X25","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X26","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X28","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ahj

Chain	Residue	Details
A	SER113
A	CYS114
B	ARG56

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 57

Chain	Residue	Details
B	ARG56	electrostatic stabiliser, proton acceptor, proton donor
B	TYR72	proton acceptor, proton donor
B	TYR76	increase acidity, increase basicity
A	PRO118	electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

---