1T60
Crystal structure of Type IV collagen NC1 domain from bovine lens capsule
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005201 | molecular_function | extracellular matrix structural constituent |
A | 0005581 | cellular_component | collagen trimer |
B | 0005201 | molecular_function | extracellular matrix structural constituent |
B | 0005581 | cellular_component | collagen trimer |
C | 0005201 | molecular_function | extracellular matrix structural constituent |
C | 0005576 | cellular_component | extracellular region |
C | 0005581 | cellular_component | collagen trimer |
C | 0005604 | cellular_component | basement membrane |
D | 0005201 | molecular_function | extracellular matrix structural constituent |
D | 0005581 | cellular_component | collagen trimer |
E | 0005201 | molecular_function | extracellular matrix structural constituent |
E | 0005581 | cellular_component | collagen trimer |
F | 0005201 | molecular_function | extracellular matrix structural constituent |
F | 0005576 | cellular_component | extracellular region |
F | 0005581 | cellular_component | collagen trimer |
F | 0005604 | cellular_component | basement membrane |
G | 0005201 | molecular_function | extracellular matrix structural constituent |
G | 0005581 | cellular_component | collagen trimer |
H | 0005201 | molecular_function | extracellular matrix structural constituent |
H | 0005581 | cellular_component | collagen trimer |
I | 0005201 | molecular_function | extracellular matrix structural constituent |
I | 0005576 | cellular_component | extracellular region |
I | 0005581 | cellular_component | collagen trimer |
I | 0005604 | cellular_component | basement membrane |
J | 0005201 | molecular_function | extracellular matrix structural constituent |
J | 0005581 | cellular_component | collagen trimer |
K | 0005201 | molecular_function | extracellular matrix structural constituent |
K | 0005581 | cellular_component | collagen trimer |
L | 0005201 | molecular_function | extracellular matrix structural constituent |
L | 0005576 | cellular_component | extracellular region |
L | 0005581 | cellular_component | collagen trimer |
L | 0005604 | cellular_component | basement membrane |
M | 0005201 | molecular_function | extracellular matrix structural constituent |
M | 0005581 | cellular_component | collagen trimer |
N | 0005201 | molecular_function | extracellular matrix structural constituent |
N | 0005581 | cellular_component | collagen trimer |
O | 0005201 | molecular_function | extracellular matrix structural constituent |
O | 0005576 | cellular_component | extracellular region |
O | 0005581 | cellular_component | collagen trimer |
O | 0005604 | cellular_component | basement membrane |
P | 0005201 | molecular_function | extracellular matrix structural constituent |
P | 0005581 | cellular_component | collagen trimer |
Q | 0005201 | molecular_function | extracellular matrix structural constituent |
Q | 0005581 | cellular_component | collagen trimer |
R | 0005201 | molecular_function | extracellular matrix structural constituent |
R | 0005576 | cellular_component | extracellular region |
R | 0005581 | cellular_component | collagen trimer |
R | 0005604 | cellular_component | basement membrane |
S | 0005201 | molecular_function | extracellular matrix structural constituent |
S | 0005581 | cellular_component | collagen trimer |
T | 0005201 | molecular_function | extracellular matrix structural constituent |
T | 0005581 | cellular_component | collagen trimer |
U | 0005201 | molecular_function | extracellular matrix structural constituent |
U | 0005576 | cellular_component | extracellular region |
U | 0005581 | cellular_component | collagen trimer |
U | 0005604 | cellular_component | basement membrane |
V | 0005201 | molecular_function | extracellular matrix structural constituent |
V | 0005581 | cellular_component | collagen trimer |
W | 0005201 | molecular_function | extracellular matrix structural constituent |
W | 0005581 | cellular_component | collagen trimer |
X | 0005201 | molecular_function | extracellular matrix structural constituent |
X | 0005576 | cellular_component | extracellular region |
X | 0005581 | cellular_component | collagen trimer |
X | 0005604 | cellular_component | basement membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K C 5101 |
Chain | Residue |
A | TYR189 |
C | TYR63 |
C | ASN65 |
E | ALA186 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K D 5102 |
Chain | Residue |
B | ALA186 |
D | TYR189 |
F | TYR63 |
F | ASN65 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K G 5103 |
Chain | Residue |
I | TYR63 |
I | ASN65 |
K | ALA186 |
G | TYR189 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K L 5104 |
Chain | Residue |
H | ALA186 |
J | TYR189 |
L | TYR63 |
L | ASN65 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K M 5105 |
Chain | Residue |
M | TYR189 |
O | TYR63 |
O | ASN65 |
Q | ALA186 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K P 5106 |
Chain | Residue |
N | ALA186 |
P | TYR189 |
R | TYR63 |
R | ASN65 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K U 5107 |
Chain | Residue |
S | TYR189 |
U | TYR63 |
U | ASN65 |
W | ALA186 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K V 5108 |
Chain | Residue |
T | ALA186 |
V | TYR189 |
X | TYR63 |
X | ASN65 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K B 5109 |
Chain | Residue |
B | ASN66 |
B | HOH5142 |
C | TYR187 |
F | TYR183 |
F | ALA184 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K C 5110 |
Chain | Residue |
C | TYR183 |
C | ALA184 |
E | ASN66 |
F | TYR187 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K H 5111 |
Chain | Residue |
H | ASN66 |
H | HOH5152 |
I | TYR187 |
L | TYR183 |
L | ALA184 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K I 5112 |
Chain | Residue |
I | ALA184 |
K | ASN66 |
K | HOH294 |
L | TYR187 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K N 5113 |
Chain | Residue |
N | ASN66 |
O | TYR187 |
R | ALA184 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K O 5114 |
Chain | Residue |
O | TYR183 |
O | ALA184 |
Q | ASN66 |
R | TYR187 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K T 5115 |
Chain | Residue |
T | ASN66 |
U | TYR187 |
X | TYR183 |
X | ALA184 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K U 5116 |
Chain | Residue |
U | TYR183 |
U | ALA184 |
W | ASN66 |
X | TYR187 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 5201 |
Chain | Residue |
A | ALA74 |
A | ARG76 |
A | ASP78 |
A | HOH5203 |
D | HOH5256 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL C 5202 |
Chain | Residue |
C | ALA73 |
C | ARG75 |
C | ASN76 |
C | ASP77 |
C | HOH5209 |
C | HOH5221 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL D 5203 |
Chain | Residue |
A | HOH5246 |
D | ALA74 |
D | ARG76 |
D | ASN77 |
D | ASP78 |
D | HOH5211 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL F 5204 |
Chain | Residue |
F | ALA73 |
F | ARG75 |
F | ASP77 |
F | HOH5224 |
F | HOH5225 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL G 5205 |
Chain | Residue |
G | ALA74 |
G | ARG76 |
G | ASP78 |
G | GLY178 |
G | HOH5215 |
J | ARG179 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL I 5206 |
Chain | Residue |
I | ALA73 |
I | ARG75 |
I | ASN76 |
I | ASP77 |
I | HOH5211 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL J 5207 |
Chain | Residue |
J | ALA74 |
J | ARG76 |
J | ASN77 |
J | ASP78 |
J | GLY178 |
J | HOH5216 |
G | ARG179 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL M 5208 |
Chain | Residue |
M | ALA74 |
M | ARG76 |
M | ASP78 |
M | GLY178 |
M | HOH5217 |
P | HOH5251 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL L 5209 |
Chain | Residue |
L | ALA73 |
L | ARG75 |
L | ASN76 |
L | ASP77 |
L | HOH5216 |
L | HOH5229 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL O 5210 |
Chain | Residue |
O | ALA73 |
O | SER74 |
O | ARG75 |
O | ASN76 |
O | ASP77 |
O | HOH5213 |
O | HOH5232 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL P 5211 |
Chain | Residue |
M | HOH5248 |
P | ALA74 |
P | ARG76 |
P | ASN77 |
P | ASP78 |
P | GLY178 |
P | HOH5230 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL R 5212 |
Chain | Residue |
R | ALA73 |
R | ARG75 |
R | ASN76 |
R | ASP77 |
R | HOH5225 |
site_id | DC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CL S 5213 |
Chain | Residue |
S | ALA74 |
S | ARG76 |
S | ASN77 |
S | ASP78 |
S | GLY178 |
S | HOH5230 |
V | ARG179 |
site_id | DC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL U 5214 |
Chain | Residue |
U | ALA73 |
U | ARG75 |
U | ASN76 |
U | ASP77 |
U | HOH5219 |
U | HOH5235 |
site_id | DC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL V 5215 |
Chain | Residue |
V | ALA74 |
V | ARG76 |
V | ASP78 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL X 5216 |
Chain | Residue |
X | ALA73 |
X | ARG75 |
X | ASN76 |
X | ASP77 |
X | HOH5242 |
site_id | DC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 5001 |
Chain | Residue |
A | HIS121 |
A | GLN129 |
A | PRO131 |
site_id | DC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD T 5002 |
Chain | Residue |
T | GLY23 |
T | LYS25 |
T | GLU112 |
site_id | DC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD M 5003 |
Chain | Residue |
M | HIS121 |
M | GLN129 |
M | HOH5316 |
site_id | DC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD S 5004 |
Chain | Residue |
S | VAL120 |
S | GLN129 |
S | PRO131 |
site_id | EC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD S 5005 |
Chain | Residue |
S | PHE168 |
S | ALA212 |
S | GLY213 |
S | LEU215 |
S | ARG216 |
U | HOH5285 |
site_id | EC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD P 5006 |
Chain | Residue |
P | VAL120 |
P | GLN129 |
R | LEU26 |
R | TRP27 |
site_id | EC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MPD D 5007 |
Chain | Residue |
D | MET89 |
D | MET93 |
D | TYR185 |
D | ALA186 |
D | HOH5262 |
F | PRO66 |
F | GLY67 |
site_id | EC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD M 5008 |
Chain | Residue |
M | MET89 |
M | MET93 |
M | ALA186 |
M | HOH5254 |
O | GLY67 |
P | ASN68 |
site_id | EC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MPD J 5009 |
Chain | Residue |
G | ASN68 |
J | MET89 |
J | MET93 |
J | TYR185 |
J | ALA186 |
L | PRO66 |
L | GLY67 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | CROSSLNK: S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651) => ECO:0000269|PubMed:19729652 |
Chain | Residue | Details |
A | MET93 | |
N | MET93 | |
P | MET93 | |
Q | MET93 | |
S | MET93 | |
T | MET93 | |
V | MET93 | |
W | MET93 | |
B | MET93 | |
D | MET93 | |
E | MET93 | |
G | MET93 | |
H | MET93 | |
J | MET93 | |
K | MET93 | |
M | MET93 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | CROSSLNK: S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533) => ECO:0000269|PubMed:19729652 |
Chain | Residue | Details |
G | LYS211 | |
H | LYS211 | |
J | LYS211 | |
K | LYS211 | |
M | LYS211 | |
A | LYS211 | |
N | LYS211 | |
P | LYS211 | |
Q | LYS211 | |
S | LYS211 | |
T | LYS211 | |
V | LYS211 | |
W | LYS211 | |
B | LYS211 | |
D | LYS211 | |
E | LYS211 |