1VLN
A TRICLINIC CRYSTAL FORM OF THE LECTIN CONCANAVALIN A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005537 | molecular_function | D-mannose binding |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0035821 | biological_process | modulation of process of another organism |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0090729 | molecular_function | toxin activity |
B | 0005537 | molecular_function | D-mannose binding |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0090729 | molecular_function | toxin activity |
C | 0005537 | molecular_function | D-mannose binding |
C | 0030246 | molecular_function | carbohydrate binding |
C | 0035821 | biological_process | modulation of process of another organism |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0090729 | molecular_function | toxin activity |
D | 0005537 | molecular_function | D-mannose binding |
D | 0030246 | molecular_function | carbohydrate binding |
D | 0035821 | biological_process | modulation of process of another organism |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0090729 | molecular_function | toxin activity |
E | 0005537 | molecular_function | D-mannose binding |
E | 0030246 | molecular_function | carbohydrate binding |
E | 0035821 | biological_process | modulation of process of another organism |
E | 0042802 | molecular_function | identical protein binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0090729 | molecular_function | toxin activity |
F | 0005537 | molecular_function | D-mannose binding |
F | 0030246 | molecular_function | carbohydrate binding |
F | 0035821 | biological_process | modulation of process of another organism |
F | 0042802 | molecular_function | identical protein binding |
F | 0046872 | molecular_function | metal ion binding |
F | 0090729 | molecular_function | toxin activity |
G | 0005537 | molecular_function | D-mannose binding |
G | 0030246 | molecular_function | carbohydrate binding |
G | 0035821 | biological_process | modulation of process of another organism |
G | 0042802 | molecular_function | identical protein binding |
G | 0046872 | molecular_function | metal ion binding |
G | 0090729 | molecular_function | toxin activity |
H | 0005537 | molecular_function | D-mannose binding |
H | 0030246 | molecular_function | carbohydrate binding |
H | 0035821 | biological_process | modulation of process of another organism |
H | 0042802 | molecular_function | identical protein binding |
H | 0046872 | molecular_function | metal ion binding |
H | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 238 |
Chain | Residue |
A | GLU8 |
A | ASP10 |
A | ASP19 |
A | HIS24 |
A | HOH240 |
A | HOH241 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 239 |
Chain | Residue |
A | ASP19 |
A | HOH242 |
A | HOH243 |
A | ASP10 |
A | TYR12 |
A | ASN14 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 238 |
Chain | Residue |
B | GLU8 |
B | ASP10 |
B | ASP19 |
B | HIS24 |
B | HOH240 |
B | HOH241 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 239 |
Chain | Residue |
B | ASP10 |
B | TYR12 |
B | ASN14 |
B | ASP19 |
B | HOH242 |
B | HOH243 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 238 |
Chain | Residue |
C | GLU8 |
C | ASP10 |
C | ASP19 |
C | HIS24 |
C | HOH240 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 239 |
Chain | Residue |
C | ASP10 |
C | TYR12 |
C | ASN14 |
C | ASP19 |
C | HOH242 |
C | HOH243 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 238 |
Chain | Residue |
D | GLU8 |
D | ASP10 |
D | ASP19 |
D | HIS24 |
D | HOH240 |
D | HOH241 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA D 239 |
Chain | Residue |
D | ASP10 |
D | TYR12 |
D | ASN14 |
D | ASP19 |
D | HOH242 |
D | HOH243 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 238 |
Chain | Residue |
E | GLU8 |
E | ASP10 |
E | ASP19 |
E | HIS24 |
E | HOH240 |
E | HOH241 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA E 239 |
Chain | Residue |
E | ASP10 |
E | TYR12 |
E | ASN14 |
E | ASP19 |
E | HOH242 |
E | HOH243 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 238 |
Chain | Residue |
F | GLU8 |
F | ASP10 |
F | ASP19 |
F | HIS24 |
F | HOH240 |
F | HOH241 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA F 239 |
Chain | Residue |
F | ASP10 |
F | TYR12 |
F | ASN14 |
F | ASP19 |
F | HOH242 |
F | HOH243 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN G 238 |
Chain | Residue |
G | GLU8 |
G | ASP10 |
G | ASP19 |
G | HIS24 |
G | HOH240 |
G | HOH241 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA G 239 |
Chain | Residue |
G | ASP10 |
G | TYR12 |
G | ASN14 |
G | ASP19 |
G | HOH242 |
G | HOH243 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN H 238 |
Chain | Residue |
H | GLU8 |
H | ASP10 |
H | ASP19 |
H | HIS24 |
H | HOH240 |
H | HOH241 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA H 239 |
Chain | Residue |
H | ASP10 |
H | TYR12 |
H | ASN14 |
H | ASP19 |
H | HOH242 |
H | HOH243 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU8 | |
B | VAL188 | |
C | GLU8 | |
C | ASP10 | |
C | ASP19 | |
C | HIS24 | |
C | VAL188 | |
D | GLU8 | |
D | ASP10 | |
D | ASP19 | |
D | HIS24 | |
A | ASP10 | |
D | VAL188 | |
E | GLU8 | |
E | ASP10 | |
E | ASP19 | |
E | HIS24 | |
E | VAL188 | |
F | GLU8 | |
F | ASP10 | |
F | ASP19 | |
F | HIS24 | |
A | ASP19 | |
F | VAL188 | |
G | GLU8 | |
G | ASP10 | |
G | ASP19 | |
G | HIS24 | |
G | VAL188 | |
H | GLU8 | |
H | ASP10 | |
H | ASP19 | |
H | HIS24 | |
A | HIS24 | |
H | VAL188 | |
A | VAL188 | |
B | GLU8 | |
B | ASP10 | |
B | ASP19 | |
B | HIS24 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8812975, ECO:0000269|PubMed:9830028 |
Chain | Residue | Details |
A | TYR12 | |
E | ASN14 | |
F | TYR12 | |
F | ASN14 | |
G | TYR12 | |
G | ASN14 | |
H | TYR12 | |
H | ASN14 | |
A | ASN14 | |
B | TYR12 | |
B | ASN14 | |
C | TYR12 | |
C | ASN14 | |
D | TYR12 | |
D | ASN14 | |
E | TYR12 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | THR123 | |
E | ASP208 | |
F | THR123 | |
F | ASP208 | |
G | THR123 | |
G | ASP208 | |
H | THR123 | |
H | ASP208 | |
A | ASP208 | |
B | THR123 | |
B | ASP208 | |
C | THR123 | |
C | ASP208 | |
D | THR123 | |
D | ASP208 | |
E | THR123 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9830028 |
Chain | Residue | Details |
A | ARG228 | |
B | ARG228 | |
C | ARG228 | |
D | ARG228 | |
E | ARG228 | |
F | ARG228 | |
G | ARG228 | |
H | ARG228 |