Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SZZ

Crystal structure of peptide deformylase from Leptospira Interrogans complexed with inhibitor actinonin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006412	biological_process	translation
A	0016787	molecular_function	hydrolase activity
A	0042586	molecular_function	peptide deformylase activity
A	0046872	molecular_function	metal ion binding
B	0006412	biological_process	translation
B	0016787	molecular_function	hydrolase activity
B	0042586	molecular_function	peptide deformylase activity
B	0046872	molecular_function	metal ion binding
C	0006412	biological_process	translation
C	0016787	molecular_function	hydrolase activity
C	0042586	molecular_function	peptide deformylase activity
C	0046872	molecular_function	metal ion binding
D	0006412	biological_process	translation
D	0016787	molecular_function	hydrolase activity
D	0042586	molecular_function	peptide deformylase activity
D	0046872	molecular_function	metal ion binding
E	0006412	biological_process	translation
E	0016787	molecular_function	hydrolase activity
E	0042586	molecular_function	peptide deformylase activity
E	0046872	molecular_function	metal ion binding
F	0006412	biological_process	translation
F	0016787	molecular_function	hydrolase activity
F	0042586	molecular_function	peptide deformylase activity
F	0046872	molecular_function	metal ion binding
G	0006412	biological_process	translation
G	0016787	molecular_function	hydrolase activity
G	0042586	molecular_function	peptide deformylase activity
G	0046872	molecular_function	metal ion binding
H	0006412	biological_process	translation
H	0016787	molecular_function	hydrolase activity
H	0042586	molecular_function	peptide deformylase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 716

Chain	Residue
A	GLN53
A	CYS101
A	HIS143
A	HIS147
A	BB2513

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 717

Chain	Residue
B	BB2514
B	GLN53
B	CYS101
B	HIS143
B	HIS147

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN C 718

Chain	Residue
C	GLN53
C	CYS101
C	HIS143
C	HIS147
C	BB2515

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN D 719

Chain	Residue
D	GLN53
D	CYS101
D	HIS143
D	HIS147
D	BB2516

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN E 720

Chain	Residue
E	GLN53
E	CYS101
E	HIS143
E	HIS147
E	BB2517

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN F 721

Chain	Residue
F	GLN53
F	CYS101
F	HIS143
F	HIS147
F	BB2518

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN G 722

Chain	Residue
G	GLN53
G	CYS101
G	HIS143
G	HIS147
G	BB2519

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN H 723

Chain	Residue
H	GLN53
H	CYS101
H	HIS143
H	HIS147
H	BB2520

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BB2 A 513

Chain	Residue
A	GLY46
A	VAL47
A	GLY48
A	GLN53
A	TRP98
A	GLY100
A	CYS101
A	LEU102
A	TYR136
A	ILE139
A	VAL140
A	HIS143
A	GLU144
A	HIS147
A	ZN716

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BB2 B 514

Chain	Residue
B	GLY46
B	VAL47
B	GLY48
B	GLN53
B	TYR71
B	PHE97
B	TRP98
B	GLY100
B	CYS101
B	LEU102
B	TYR136
B	ILE139
B	VAL140
B	HIS143
B	GLU144
B	HIS147
B	ZN717

site_id	BC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BB2 C 515

Chain	Residue
C	GLY46
C	VAL47
C	GLY48
C	GLN53
C	TYR71
C	TRP98
C	GLU99
C	GLY100
C	CYS101
C	LEU102
C	TYR136
C	ILE139
C	HIS143
C	GLU144
C	HIS147
C	ZN718

site_id	BC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BB2 D 516

Chain	Residue
D	TYR136
D	VAL140
D	HIS143
D	GLU144
D	HIS147
D	ZN719
D	GLY46
D	VAL47
D	GLY48
D	GLN53
D	GLU69
D	THR74
D	TRP98
D	GLU99
D	GLY100
D	CYS101
D	LEU102

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BB2 E 517

Chain	Residue
E	GLY46
E	VAL47
E	GLY48
E	GLN53
E	TRP98
E	GLU99
E	GLY100
E	CYS101
E	LEU102
E	ILE139
E	HIS143
E	GLU144
E	HIS147
E	ZN720

site_id	BC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BB2 F 518

Chain	Residue
F	GLY46
F	VAL47
F	GLY48
F	GLN53
F	TRP98
F	GLY100
F	CYS101
F	LEU102
F	TYR136
F	HIS143
F	GLU144
F	HIS147
F	ZN721

site_id	BC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BB2 G 519

Chain	Residue
G	VAL47
G	GLY48
G	GLN53
G	PHE97
G	TRP98
G	GLU99
G	GLY100
G	CYS101
G	LEU102
G	ILE139
G	VAL140
G	HIS143
G	GLU144
G	HIS147
G	ZN722

site_id	BC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BB2 H 520

Chain	Residue
H	GLY46
H	VAL47
H	GLY48
H	GLN53
H	TRP98
H	GLY100
H	CYS101
H	LEU102
H	ARG108
H	TYR136
H	VAL140
H	HIS143
H	GLU144
H	HIS147
H	ZN723

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00163","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00163","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
A	LEU102
A	GLY48
A	GLN53
A	GLU144

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
B	LEU102
B	GLY48
B	GLN53
B	GLU144

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
C	LEU102
C	GLY48
C	GLN53
C	GLU144

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
D	LEU102
D	GLY48
D	GLN53
D	GLU144

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
E	LEU102
E	GLY48
E	GLN53
E	GLU144

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
F	LEU102
F	GLY48
F	GLN53
F	GLU144

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
G	LEU102
G	GLY48
G	GLN53
G	GLU144

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1bs4

Chain	Residue	Details
H	LEU102
H	GLY48
H	GLN53
H	GLU144

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