6VYP
Crystal structure of the LSD1/CoREST histone demethylase bound to its nucleosome substrate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000786 | cellular_component | nucleosome |
A | 0003677 | molecular_function | DNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005694 | cellular_component | chromosome |
A | 0030527 | molecular_function | structural constituent of chromatin |
A | 0046982 | molecular_function | protein heterodimerization activity |
B | 0000786 | cellular_component | nucleosome |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005694 | cellular_component | chromosome |
B | 0006334 | biological_process | nucleosome assembly |
B | 0030527 | molecular_function | structural constituent of chromatin |
B | 0046982 | molecular_function | protein heterodimerization activity |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0046982 | molecular_function | protein heterodimerization activity |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005694 | cellular_component | chromosome |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0046982 | molecular_function | protein heterodimerization activity |
E | 0000786 | cellular_component | nucleosome |
E | 0003677 | molecular_function | DNA binding |
E | 0005515 | molecular_function | protein binding |
E | 0005634 | cellular_component | nucleus |
E | 0005654 | cellular_component | nucleoplasm |
E | 0005694 | cellular_component | chromosome |
E | 0030527 | molecular_function | structural constituent of chromatin |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0000786 | cellular_component | nucleosome |
F | 0003677 | molecular_function | DNA binding |
F | 0005515 | molecular_function | protein binding |
F | 0005634 | cellular_component | nucleus |
F | 0005694 | cellular_component | chromosome |
F | 0006334 | biological_process | nucleosome assembly |
F | 0030527 | molecular_function | structural constituent of chromatin |
F | 0046982 | molecular_function | protein heterodimerization activity |
G | 0000786 | cellular_component | nucleosome |
G | 0003677 | molecular_function | DNA binding |
G | 0005634 | cellular_component | nucleus |
G | 0005694 | cellular_component | chromosome |
G | 0030527 | molecular_function | structural constituent of chromatin |
G | 0046982 | molecular_function | protein heterodimerization activity |
H | 0000786 | cellular_component | nucleosome |
H | 0003677 | molecular_function | DNA binding |
H | 0005515 | molecular_function | protein binding |
H | 0005634 | cellular_component | nucleus |
H | 0005694 | cellular_component | chromosome |
H | 0030527 | molecular_function | structural constituent of chromatin |
H | 0046982 | molecular_function | protein heterodimerization activity |
K | 0005634 | cellular_component | nucleus |
K | 0006355 | biological_process | regulation of DNA-templated transcription |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
M | 0005634 | cellular_component | nucleus |
M | 0006355 | biological_process | regulation of DNA-templated transcription |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0050660 | molecular_function | flavin adenine dinucleotide binding |
a | 0000786 | cellular_component | nucleosome |
a | 0003677 | molecular_function | DNA binding |
a | 0005515 | molecular_function | protein binding |
a | 0005634 | cellular_component | nucleus |
a | 0005654 | cellular_component | nucleoplasm |
a | 0005694 | cellular_component | chromosome |
a | 0030527 | molecular_function | structural constituent of chromatin |
a | 0046982 | molecular_function | protein heterodimerization activity |
b | 0000786 | cellular_component | nucleosome |
b | 0003677 | molecular_function | DNA binding |
b | 0005515 | molecular_function | protein binding |
b | 0005634 | cellular_component | nucleus |
b | 0005694 | cellular_component | chromosome |
b | 0006334 | biological_process | nucleosome assembly |
b | 0030527 | molecular_function | structural constituent of chromatin |
b | 0046982 | molecular_function | protein heterodimerization activity |
c | 0000786 | cellular_component | nucleosome |
c | 0003677 | molecular_function | DNA binding |
c | 0005634 | cellular_component | nucleus |
c | 0005694 | cellular_component | chromosome |
c | 0030527 | molecular_function | structural constituent of chromatin |
c | 0046982 | molecular_function | protein heterodimerization activity |
d | 0000786 | cellular_component | nucleosome |
d | 0003677 | molecular_function | DNA binding |
d | 0005515 | molecular_function | protein binding |
d | 0005634 | cellular_component | nucleus |
d | 0005694 | cellular_component | chromosome |
d | 0030527 | molecular_function | structural constituent of chromatin |
d | 0046982 | molecular_function | protein heterodimerization activity |
e | 0000786 | cellular_component | nucleosome |
e | 0003677 | molecular_function | DNA binding |
e | 0005515 | molecular_function | protein binding |
e | 0005634 | cellular_component | nucleus |
e | 0005654 | cellular_component | nucleoplasm |
e | 0005694 | cellular_component | chromosome |
e | 0030527 | molecular_function | structural constituent of chromatin |
e | 0046982 | molecular_function | protein heterodimerization activity |
f | 0000786 | cellular_component | nucleosome |
f | 0003677 | molecular_function | DNA binding |
f | 0005515 | molecular_function | protein binding |
f | 0005634 | cellular_component | nucleus |
f | 0005694 | cellular_component | chromosome |
f | 0006334 | biological_process | nucleosome assembly |
f | 0030527 | molecular_function | structural constituent of chromatin |
f | 0046982 | molecular_function | protein heterodimerization activity |
g | 0000786 | cellular_component | nucleosome |
g | 0003677 | molecular_function | DNA binding |
g | 0005634 | cellular_component | nucleus |
g | 0005694 | cellular_component | chromosome |
g | 0030527 | molecular_function | structural constituent of chromatin |
g | 0046982 | molecular_function | protein heterodimerization activity |
h | 0000786 | cellular_component | nucleosome |
h | 0003677 | molecular_function | DNA binding |
h | 0005515 | molecular_function | protein binding |
h | 0005634 | cellular_component | nucleus |
h | 0005694 | cellular_component | chromosome |
h | 0030527 | molecular_function | structural constituent of chromatin |
h | 0046982 | molecular_function | protein heterodimerization activity |
k | 0005634 | cellular_component | nucleus |
k | 0006355 | biological_process | regulation of DNA-templated transcription |
k | 0016491 | molecular_function | oxidoreductase activity |
k | 0050660 | molecular_function | flavin adenine dinucleotide binding |
m | 0005634 | cellular_component | nucleus |
m | 0006355 | biological_process | regulation of DNA-templated transcription |
m | 0016491 | molecular_function | oxidoreductase activity |
m | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | binding site for residue FAD M 900 |
Chain | Residue |
E | MET4 |
M | GLY315 |
M | ARG316 |
M | VAL317 |
M | GLY330 |
M | ALA331 |
M | VAL333 |
M | VAL590 |
M | THR624 |
M | LEU625 |
M | PRO626 |
M | GLY285 |
M | LEU659 |
M | TRP756 |
M | SER760 |
M | TYR761 |
M | GLY800 |
M | GLU801 |
M | THR810 |
M | VAL811 |
M | ALA814 |
M | GLY287 |
M | VAL288 |
M | SER289 |
M | GLU308 |
M | ALA309 |
M | ARG310 |
M | GLY314 |
site_id | AC2 |
Number of Residues | 31 |
Details | binding site for Di-peptide FAD K 900 and ARG K 310 |
Chain | Residue |
K | GLY285 |
K | GLY287 |
K | VAL288 |
K | SER289 |
K | LEU307 |
K | GLU308 |
K | ALA309 |
K | ASP311 |
K | ARG312 |
K | GLY314 |
K | GLY315 |
K | ARG316 |
K | GLY330 |
K | ALA331 |
K | MET332 |
K | VAL333 |
K | VAL334 |
K | LEU586 |
K | ASN587 |
K | THR624 |
K | LEU625 |
K | ASP754 |
K | TRP756 |
K | SER760 |
K | TYR761 |
K | GLY800 |
K | GLU801 |
K | ALA809 |
K | THR810 |
K | VAL811 |
K | ALA814 |
site_id | AC3 |
Number of Residues | 29 |
Details | binding site for Di-peptide FAD K 900 and GLY K 315 |
Chain | Residue |
K | GLY285 |
K | GLY287 |
K | VAL288 |
K | SER289 |
K | LEU307 |
K | GLU308 |
K | ALA309 |
K | ARG310 |
K | ARG312 |
K | VAL313 |
K | GLY314 |
K | ARG316 |
K | VAL317 |
K | GLY330 |
K | ALA331 |
K | MET332 |
K | VAL333 |
K | VAL334 |
K | THR624 |
K | LEU625 |
K | TRP756 |
K | SER760 |
K | TYR761 |
K | GLY800 |
K | GLU801 |
K | ALA809 |
K | THR810 |
K | VAL811 |
K | ALA814 |
site_id | AC4 |
Number of Residues | 29 |
Details | binding site for Di-peptide FAD K 900 and GLY K 330 |
Chain | Residue |
K | ASP328 |
K | LEU329 |
K | ALA331 |
K | MET332 |
K | VAL333 |
K | VAL334 |
K | THR624 |
K | LEU625 |
K | TRP751 |
K | TRP756 |
K | SER760 |
K | TYR761 |
K | GLY800 |
K | GLU801 |
K | ALA809 |
K | THR810 |
K | VAL811 |
K | ALA814 |
K | GLY285 |
K | GLY287 |
K | VAL288 |
K | SER289 |
K | LEU307 |
K | GLU308 |
K | ALA309 |
K | ARG310 |
K | GLY314 |
K | GLY315 |
K | ARG316 |
site_id | AC5 |
Number of Residues | 28 |
Details | binding site for Di-peptide FAD K 900 and VAL K 333 |
Chain | Residue |
K | GLY285 |
K | GLY287 |
K | VAL288 |
K | SER289 |
K | LEU307 |
K | GLU308 |
K | ALA309 |
K | ARG310 |
K | GLY314 |
K | GLY315 |
K | ARG316 |
K | GLY330 |
K | ALA331 |
K | MET332 |
K | VAL334 |
K | LEU565 |
K | THR566 |
K | THR624 |
K | LEU625 |
K | TRP756 |
K | SER760 |
K | TYR761 |
K | GLY800 |
K | GLU801 |
K | ALA809 |
K | THR810 |
K | VAL811 |
K | ALA814 |
site_id | AC6 |
Number of Residues | 29 |
Details | binding site for Di-peptide FAD k 900 and ALA k 331 |
Chain | Residue |
k | GLY285 |
k | SER286 |
k | GLY287 |
k | VAL288 |
k | SER289 |
k | GLU308 |
k | ALA309 |
k | ARG310 |
k | GLY314 |
k | GLY315 |
k | ARG316 |
k | GLY330 |
k | MET332 |
k | VAL333 |
k | VAL590 |
k | THR624 |
k | LEU625 |
k | PRO626 |
k | VAL629 |
k | LEU659 |
k | TRP756 |
k | SER760 |
k | TYR761 |
k | GLY800 |
k | GLU801 |
k | THR810 |
k | VAL811 |
k | HIS812 |
k | ALA814 |
site_id | AC7 |
Number of Residues | 31 |
Details | binding site for Di-peptide FAD k 900 and VAL k 811 |
Chain | Residue |
k | GLY285 |
k | SER286 |
k | GLY287 |
k | VAL288 |
k | SER289 |
k | GLU308 |
k | ALA309 |
k | ARG310 |
k | GLY314 |
k | GLY315 |
k | ARG316 |
k | ALA331 |
k | MET332 |
k | VAL333 |
k | TYR571 |
k | VAL590 |
k | THR624 |
k | LEU625 |
k | PRO626 |
k | VAL629 |
k | LEU659 |
k | TRP756 |
k | SER760 |
k | TYR761 |
k | GLY800 |
k | GLU801 |
k | THR810 |
k | HIS812 |
k | GLY813 |
k | ALA814 |
k | LEU815 |
site_id | AC8 |
Number of Residues | 34 |
Details | binding site for Di-peptide FAD k 900 and HIS k 812 |
Chain | Residue |
k | GLY285 |
k | SER286 |
k | GLY287 |
k | VAL288 |
k | SER289 |
k | GLU308 |
k | ALA309 |
k | ARG310 |
k | GLY314 |
k | GLY315 |
k | ARG316 |
k | ALA331 |
k | MET332 |
k | VAL333 |
k | THR335 |
k | ASN340 |
k | MET342 |
k | VAL590 |
k | THR624 |
k | LEU625 |
k | PRO626 |
k | VAL629 |
k | LEU659 |
k | TRP756 |
k | SER760 |
k | TYR761 |
k | GLY800 |
k | GLU801 |
k | THR810 |
k | VAL811 |
k | GLY813 |
k | ALA814 |
k | LEU815 |
k | LEU816 |
site_id | AC9 |
Number of Residues | 33 |
Details | binding site for Di-peptide FAD k 900 and ALA k 814 |
Chain | Residue |
k | GLY285 |
k | SER286 |
k | GLY287 |
k | VAL288 |
k | SER289 |
k | GLU308 |
k | ALA309 |
k | ARG310 |
k | GLY314 |
k | GLY315 |
k | ARG316 |
k | ALA331 |
k | MET332 |
k | VAL333 |
k | VAL590 |
k | THR624 |
k | LEU625 |
k | PRO626 |
k | VAL629 |
k | LEU659 |
k | TRP756 |
k | SER760 |
k | TYR761 |
k | GLY800 |
k | GLU801 |
k | THR810 |
k | VAL811 |
k | HIS812 |
k | GLY813 |
k | LEU815 |
k | LEU816 |
k | SER817 |
k | GLY818 |
site_id | AD1 |
Number of Residues | 29 |
Details | binding site for Di-peptide FAD m 900 and GLY m 330 |
Chain | Residue |
m | GLY285 |
m | SER286 |
m | GLY287 |
m | VAL288 |
m | SER289 |
m | GLU308 |
m | ALA309 |
m | ARG310 |
m | GLY314 |
m | GLY315 |
m | ARG316 |
m | VAL317 |
m | ALA318 |
m | ASP328 |
m | LEU329 |
m | ALA331 |
m | VAL333 |
m | VAL590 |
m | THR624 |
m | LEU625 |
m | PRO626 |
m | LYS661 |
m | TRP751 |
m | TRP756 |
m | GLY800 |
m | GLU801 |
m | THR810 |
m | VAL811 |
m | ALA814 |
Functional Information from PROSITE/UniProt
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
Chain | Residue | Details |
C | ALA21-VAL27 |
site_id | PS00047 |
Number of Residues | 5 |
Details | HISTONE_H4 Histone H4 signature. GAKRH |
Chain | Residue | Details |
B | GLY14-HIS18 |
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
A | LYS14-LEU20 |
site_id | PS00959 |
Number of Residues | 9 |
Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
Chain | Residue | Details |
A | PRO66-ILE74 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG89-GLY111 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | MOD_RES: Citrulline; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
K | ARG310 | |
K | ARG316 | |
K | MET332 | |
K | GLU801 | |
K | THR810 | |
k | SER289 | |
k | GLU308 | |
k | ARG310 | |
k | ARG316 | |
k | MET332 | |
k | GLU801 | |
k | THR810 | |
A | ARG2 | |
A | ARG17 | |
E | ARG2 | |
E | ARG17 | |
a | ARG2 | |
a | ARG17 | |
e | ARG2 | |
e | ARG17 | |
m | GLU308 | |
m | ARG310 | |
m | ARG316 | |
m | MET332 | |
m | GLU801 | |
m | THR810 | |
K | SER289 | |
K | GLU308 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by HASPIN => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR3 | |
E | THR3 | |
a | THR3 | |
e | THR3 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12138181 |
Chain | Residue | Details |
A | MET4 | |
E | MET4 | |
a | MET4 | |
e | MET4 | |
c | LYS9 | |
c | LYS95 | |
g | LYS9 | |
g | LYS95 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
K | LYS469 | |
k | LYS469 | |
A | GLN5 | |
E | GLN5 | |
a | GLN5 | |
e | GLN5 | |
K | LYS442 | |
k | LYS442 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | THR6 | |
A | THR11 | |
E | THR6 | |
E | THR11 | |
a | THR6 | |
a | THR11 | |
e | THR6 | |
e | THR11 | |
b | LYS8 | |
b | LYS16 | |
b | LYS44 | |
b | LYS79 | |
f | LYS8 | |
f | LYS16 | |
f | LYS44 | |
f | LYS79 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250 |
Chain | Residue | Details |
A | ARG8 | |
E | ARG8 | |
a | ARG8 | |
e | ARG8 | |
b | LYS12 | |
b | LYS20 | |
f | LYS12 | |
f | LYS20 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000305|PubMed:12138181 |
Chain | Residue | Details |
A | LYS9 | |
E | LYS9 | |
a | LYS9 | |
e | LYS9 | |
b | LYS31 | |
b | LYS91 | |
f | LYS31 | |
f | LYS91 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
g | LYS13 | |
g | LYS15 | |
g | LYS119 | |
A | SER10 | |
E | SER10 | |
a | SER10 | |
e | SER10 | |
G | LYS13 | |
G | LYS15 | |
G | LYS119 | |
c | LYS13 | |
c | LYS15 | |
c | LYS119 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
A | LYS14 | |
E | LYS14 | |
a | LYS14 | |
e | LYS14 | |
b | TYR51 | |
b | TYR88 | |
f | TYR51 | |
f | TYR88 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
E | LYS64 | |
a | LYS18 | |
a | LYS23 | |
a | LYS27 | |
a | LYS36 | |
a | LYS64 | |
e | LYS18 | |
e | LYS23 | |
e | LYS27 | |
e | LYS36 | |
e | LYS64 | |
A | LYS64 | |
E | LYS18 | |
E | LYS23 | |
E | LYS27 | |
E | LYS36 | |
A | LYS18 | |
A | LYS23 | |
A | LYS27 | |
A | LYS36 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
Details | MOD_RES: Citrulline => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | ARG26 | |
E | ARG26 | |
a | ARG26 | |
e | ARG26 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER28 | |
E | SER28 | |
a | SER28 | |
e | SER28 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
b | LYS91 | |
f | LYS91 | |
A | LYS37 | |
E | LYS37 | |
a | LYS37 | |
e | LYS37 |
site_id | SWS_FT_FI14 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | TYR41 | |
E | TYR41 | |
a | TYR41 | |
e | TYR41 |
site_id | SWS_FT_FI15 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 |
Chain | Residue | Details |
a | LYS56 | |
a | LYS79 | |
e | LYS56 | |
e | LYS79 | |
A | LYS56 | |
A | LYS79 | |
E | LYS56 | |
E | LYS79 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | SER57 | |
E | SER57 | |
a | SER57 | |
e | SER57 |
site_id | SWS_FT_FI17 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
a | THR80 | |
a | THR107 | |
e | THR80 | |
e | THR107 | |
A | THR80 | |
A | THR107 | |
E | THR80 | |
E | THR107 |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243 |
Chain | Residue | Details |
A | SER86 | |
E | SER86 | |
a | SER86 | |
e | SER86 |
site_id | SWS_FT_FI19 |
Number of Residues | 4 |
Details | MOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS115 | |
E | LYS115 | |
a | LYS115 | |
e | LYS115 |
site_id | SWS_FT_FI20 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | LYS122 | |
E | LYS122 | |
a | LYS122 | |
e | LYS122 |
site_id | SWS_FT_FI21 |
Number of Residues | 4 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 |
Chain | Residue | Details |
A | CYS110 | |
E | CYS110 | |
a | CYS110 | |
e | CYS110 |