Protein Geometry Database

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Residues
Resolution	-
R-factor	-
R-free	-
Threshold
PDB Codes

	-4	-3	-2	-1	i	+1	+2	+3	+4	+5
Composition ↓
	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val	Ala Arg Asn Asp Cys Gln Glu Gly His Ile Leu Lys Met Phe Pro Ser Thr Trp Tyr Val
Conformation ↓
	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix	α helix 3₁₀ helix β sheet Turn Bend β-bridge π helix
Φ
Ψ
ω
Mobility →
B^m
B^γ
B^sc
Angles →
C^-1NC^α
NC^αC^β
NC^αC
C^βC^αC
C^αCO
C^αCN⁺¹
OCN⁺¹
Lengths →
C^-1N
NC^α
C^αC^β
C^aC
CO
χ Angles →
χ₁
χ₂
χ₃
χ₄
χ₅
Sidechain Angles →
CYS: C^αC^βS^γ
ILE: C^αC^βC^γ2
ILE: C^αC^βC^γ1
ILE: C^γ1C^βC^γ2
ILE: C^βC^γ1C^δ1
SER: C^αC^βO^γ
GLN: C^αC^βC^γ
GLN: C^βC^γC^δ
GLN: C^γC^δO^ε1
GLN: C^γC^δN^ε2
GLN: O^ε1C^δN^ε2
LYS: C^αC^βC^γ
LYS: C^βC^γC^δ
LYS: C^γC^δC^ε
LYS: C^δC^εN^ζ
TRP: C^αC^βC^γ
TRP: C^βC^γC^δ1
TRP: C^βC^γC^δ2
TRP: C^δ2C^γC^δ1
TRP: C^γC^δ1N^ε1
TRP: C^δ1N^ε1C^ε2
TRP: N^ε1C^ε2C^δ2
TRP: C^γC^δ2C^ε2
TRP: C^ε2C^δ2C^ε3
TRP: C^δ2C^ε2C^ζ2
TRP: C^ε2C^ζ2C^η2
TRP: C^ζ2C^η2C^ζ3
TRP: C^ε3C^ζ3C^η2
TRP: C^δ2C^ε3C^ζ3
TRP: C^γC^δ2C^ε3
TRP: N^ε1C^ε2C^ζ2
PRO: C^αC^βC^γ
PRO: C^βC^γC^δ
PRO: C^γC^δN
PRO: C^δNC^α
PRO: C^δNC^-1
THR: C^αC^βO^γ1
THR: C^αC^βC^γ2
THR: O^γ1C^βC^γ2
PHE: C^αC^βC^γ
PHE: C^βC^γC^δ1
PHE: C^βC^γC^δ2
PHE: C^δ1C^γC^δ2
PHE: C^ε1C^ζC^ε2
PHE: C^γC^δ1C^ε1
PHE: C^γC^δ2C^ε2
PHE: C^ζC^ε1C^δ1
PHE: C^ζC^ε2C^δ2
ASN: C^αC^βC^γ
ASN: C^βC^γO^δ1
ASN: C^βC^γN^δ2
ASN: O^δ1C^γN^δ2
MET: C^αC^βC^γ
MET: C^βC^γS^δ
MET: C^γS^δC^ε
HIS: C^αC^βC^γ
HIS: C^βC^γC^δ2
HIS: C^βC^γN^δ1
HIS: N^δ1C^γC^δ2
HIS: C^γN^δ1C^ε1
HIS: N^δ1C^ε1N^ε2
HIS: C^ε1N^ε2C^δ2
HIS: C^γC^δ2N^ε2
LEU: C^αC^βC^γ
LEU: C^βC^γC^δ1
LEU: C^βC^γC^δ2
LEU: C^δ1C^γC^δ2
ARG: C^αC^βC^γ
ARG: C^βC^γC^δ
ARG: C^γC^δN^ε
ARG: C^δN^εC^ζ
ARG: N^εC^ζN^η1
ARG: N^εC^ζN^η2
ARG: N^η1C^ζN^η2
ASP: C^αC^βC^γ
ASP: C^βC^γO^δ1
ASP: C^βC^γO^δ2
ASP: O^δ1C^γO^δ2
VAL: C^αC^βC^γ1
VAL: C^αC^βC^γ2
VAL: C^γ1C^βC^γ2
GLU: C^αC^βC^γ
GLU: C^βC^γC^δ
GLU: C^γC^δO^ε1
GLU: C^γC^δO^ε2
GLU: O^ε1C^δO^ε2
TYR: C^αC^βC^γ
TYR: C^βC^γC^δ1
TYR: C^βC^γC^δ2
TYR: C^δ1C^γC^δ2
TYR: C^ε1C^ζC^ε2
TYR: C^γC^δ1C^ε1
TYR: C^γC^δ2C^ε2
TYR: C^ζC^ε1C^δ1
TYR: C^ζC^ε2C^δ2
TYR: C^ε1C^ζO^η
TYR: C^ε2C^ζO^η
Sidechain Lengths →
CYS: C^βS^γ
ILE: C^βC^γ1
ILE: C^γ1C^δ1
ILE: C^βC^γ2
SER: C^βO^γ
GLN: C^βC^γ
GLN: C^γC^δ
GLN: C^δO^ε1
GLN: C^δN^ε2
LYS: C^βC^γ
LYS: C^γC^δ
LYS: C^δC^ε
LYS: C^εN^ζ
TRP: C^βC^γ
TRP: C^γC^δ1
TRP: C^δ1N^ε1
TRP: N^ε1C^ε2
TRP: C^ε2C^ζ2
TRP: C^ζ2C^η2
TRP: C^η2C^ζ3
TRP: C^ζ3C^ε3
TRP: C^δ2C^ε3
TRP: C^γC^δ2
TRP: C^δ2C^ε2
PRO: C^βC^γ
PRO: C^γC^δ
PRO: C^δN
THR: C^βO^γ1
THR: C^βC^γ2
PHE: C^βC^γ
PHE: C^γC^δ1
PHE: C^γC^δ2
PHE: C^δ1C^ε1
PHE: C^δ2C^ε2
PHE: C^ζC^ε1
PHE: C^ζC^ε2
ASN: C^βC^γ
ASN: C^γO^δ1
ASN: C^γN^δ2
MET: C^βC^γ
MET: C^γS^δ
MET: S^δC^ε
HIS: C^βC^γ
HIS: C^γN^δ1
HIS: N^δ1C^ε1
HIS: C^ε1N^ε2
HIS: N^ε2C^δ2
HIS: C^γC^δ2
LEU: C^βC^γ
LEU: C^γC^δ1
LEU: C^γC^δ2
ARG: C^βC^γ
ARG: C^δN^ε
ARG: C^γC^δ
ARG: N^εC^ζ
ARG: C^ζN^η1
ARG: C^ζN^η2
ASP: C^βC^γ
ASP: C^γO^δ1
ASP: C^γO^δ2
VAL: C^βC^γ1
VAL: C^βC^γ2
GLU: C^βC^γ
GLU: C^γC^δ
GLU: C^δO^ε1
GLU: C^δO^ε2
TYR: C^βC^γ
TYR: C^γC^δ1
TYR: C^γC^δ2
TYR: C^δ1C^ε1
TYR: C^δ2C^ε2
TYR: C^ζC^ε1
TYR: C^ζC^ε2
TYR: C^ζO^η

Protein Help

Search only these proteins, or exclude these proteins from the full data set

How many residues are in your search motif

The best crystallographic resolution to allow

The worst crystallographic resolution to allow

No two chains can have more than this percentage sequence identity. Lower numbers are more restrictive.

Minimum crystallographic R-factor

Maximum crystallographic R-factor

Minimum crystallographic R-free

Maximum crystallographic R-free

Peptide Help

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Secondary Structure Help

Which secondary-structure types are searched? The default is all of them.

This is Residue Properties Help

The average main-chain B-factor

The B-factor of the γ-carbon (which determines whether the χ1 sidechain dihedral angle is well-defined)

The average side-chain B-factor

ω defines the planarity of the peptide bond and generally stays close to 180° (for trans peptides) or 0° (for cis peptides)

Angles Help

Chi Help

χ₁ properties vary depending on the residue. Visit the chi help page (link here) for more information.

χ₂ properties vary depending on the residue. Visit the chi help page (link here) for more information.

χ₃ properties vary depending on the residue. Visit the chi help page (link here) for more information.

χ₄ properties vary depending on the residue. Visit the chi help page (link here) for more information.

χ₅ properties vary depending on the residue. Visit the chi help page (link here) for more information.

Lengths Help