Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1AHJ

NITRILE HYDRATASE

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
C	0003824	molecular_function	catalytic activity
C	0016829	molecular_function	lyase activity
C	0018822	molecular_function	nitrile hydratase activity
C	0046872	molecular_function	metal ion binding
C	0046914	molecular_function	transition metal ion binding
D	0016829	molecular_function	lyase activity
D	0018822	molecular_function	nitrile hydratase activity
D	0046914	molecular_function	transition metal ion binding
E	0003824	molecular_function	catalytic activity
E	0016829	molecular_function	lyase activity
E	0018822	molecular_function	nitrile hydratase activity
E	0046872	molecular_function	metal ion binding
E	0046914	molecular_function	transition metal ion binding
F	0016829	molecular_function	lyase activity
F	0018822	molecular_function	nitrile hydratase activity
F	0046914	molecular_function	transition metal ion binding
G	0003824	molecular_function	catalytic activity
G	0016829	molecular_function	lyase activity
G	0018822	molecular_function	nitrile hydratase activity
G	0046872	molecular_function	metal ion binding
G	0046914	molecular_function	transition metal ion binding
H	0016829	molecular_function	lyase activity
H	0018822	molecular_function	nitrile hydratase activity
H	0046914	molecular_function	transition metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE C 208

Chain	Residue
C	CYS110
C	CYS113
C	SER114
C	CYS115

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 208

Chain	Residue
A	CYS110
A	CYS113
A	SER114
A	CYS115

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 208

Chain	Residue
E	CYS110
E	CYS113
E	SER114
E	CYS115

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE G 208

Chain	Residue
G	CYS110
G	CYS113
G	SER114
G	CYS115

site_id	FEA
Number of Residues	4
Details	IRON BINDING SITE.

Chain	Residue
A	CYS110
A	CYS113
A	SER114
C	CYS115

site_id	FEC
Number of Residues	4
Details	IRON BINDING SITE.

Chain	Residue
C	CYS110
C	CYS113
C	SER114
C	CYS115

site_id	FEE
Number of Residues	4
Details	IRON BINDING SITE.

Chain	Residue
E	CYS113
E	SER114
C	CYS115
E	CYS110

site_id	FEG
Number of Residues	4
Details	IRON BINDING SITE.

Chain	Residue
G	CYS110
G	CYS113
G	SER114
C	CYS115

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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	8
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	4
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	4
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	4
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	4
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	4
Details	a catalytic site defined by CSA, PubMed 10679370, 11001100, 9195885, 9586994

Chain	Residue	Details
A	CYS113
A	SER114
A	CYS115
B	ARG56

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10679370, 11001100, 9195885, 9586994

Chain	Residue	Details
D	ARG56
C	CYS113
C	SER114
C	CYS115

site_id	CSA3
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10679370, 11001100, 9195885, 9586994

Chain	Residue	Details
F	ARG56
E	CYS113
E	SER114
E	CYS115

site_id	CSA4
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 10679370, 11001100, 9195885, 9586994

Chain	Residue	Details
H	ARG56
G	CYS113
G	SER114
G	CYS115

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	CYS115	electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	3
Details	M-CSA 57

Chain	Residue	Details
D	ARG56	electrostatic stabiliser, proton acceptor, proton donor
D	TYR72	proton acceptor, proton donor
D	TYR76	increase acidity, increase basicity
C	CYS115	electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

site_id	MCSA3
Number of Residues	3
Details	M-CSA 57

Chain	Residue	Details
F	ARG56	electrostatic stabiliser, proton acceptor, proton donor
F	TYR72	proton acceptor, proton donor
F	TYR76	increase acidity, increase basicity
E	CYS115	electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

site_id	MCSA4
Number of Residues	3
Details	M-CSA 57

Chain	Residue	Details
H	ARG56	electrostatic stabiliser, proton acceptor, proton donor
H	TYR72	proton acceptor, proton donor
H	TYR76	increase acidity, increase basicity
G	CYS115	electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)