eF-site ID 5vmp-C
PDB Code 5vmp
Chain C

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Title Crystal Structure of Human KDM4 with Small Molecule Inhibitor QC5714
Classification OXIDOREDUCTASE/INHIBITOR
Compound Lysine-specific demethylase 4A
Source Homo sapiens (Human) (KDM4A_HUMAN)
Sequence C:  ARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPK
EWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKA
MTVREFRKIANSDKYCTPRYFEELERKYWKNLTFNPPIYG
ADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNT
PYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPP
EHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKY
GIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFAT
RRWIEYGKQAVLCSCRKISMDVFVRKFQPERYKLWKAGKT
VIDHTLPTPEAAEFL
Description


Functional site

1) chain C
residue 188
type
sequence H
description binding site for residue NI C 501
source : AC7

2) chain C
residue 190
type
sequence E
description binding site for residue NI C 501
source : AC7

3) chain C
residue 276
type
sequence H
description binding site for residue NI C 501
source : AC7

4) chain C
residue 234
type
sequence C
description binding site for residue ZN C 502
source : AC8

5) chain C
residue 240
type
sequence H
description binding site for residue ZN C 502
source : AC8

6) chain C
residue 306
type
sequence C
description binding site for residue ZN C 502
source : AC8

7) chain C
residue 308
type
sequence C
description binding site for residue ZN C 502
source : AC8

8) chain C
residue 73
type
sequence Q
description binding site for residue 9FJ C 503
source : AC9

9) chain C
residue 86
type
sequence N
description binding site for residue 9FJ C 503
source : AC9

10) chain C
residue 132
type
sequence Y
description binding site for residue 9FJ C 503
source : AC9

11) chain C
residue 184
type
sequence S
description binding site for residue 9FJ C 503
source : AC9

12) chain C
residue 185
type
sequence F
description binding site for residue 9FJ C 503
source : AC9

13) chain C
residue 188
type
sequence H
description binding site for residue 9FJ C 503
source : AC9

14) chain C
residue 206
type
sequence K
description binding site for residue 9FJ C 503
source : AC9

15) chain C
residue 208
type
sequence W
description binding site for residue 9FJ C 503
source : AC9

16) chain C
residue 240
type
sequence H
description binding site for residue 9FJ C 503
source : AC9

17) chain C
residue 276
type
sequence H
description binding site for residue 9FJ C 503
source : AC9

18) chain C
residue 170
type catalytic
sequence G
description 370
source MCSA : MCSA3

19) chain C
residue 177
type catalytic
sequence Y
description 370
source MCSA : MCSA3

20) chain C
residue 188
type catalytic
sequence H
description 370
source MCSA : MCSA3

21) chain C
residue 190
type catalytic
sequence E
description 370
source MCSA : MCSA3

22) chain C
residue 276
type catalytic
sequence H
description 370
source MCSA : MCSA3

23) chain C
residue 288
type catalytic
sequence S
description 370
source MCSA : MCSA3

24) chain C
residue 241
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:B2RXH2
source Swiss-Prot : SWS_FT_FI5

25) chain C
residue 132
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:16677698
source Swiss-Prot : SWS_FT_FI1

26) chain C
residue 198
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16677698
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 206
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:16677698
source Swiss-Prot : SWS_FT_FI1

28) chain C
residue 188
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168
source Swiss-Prot : SWS_FT_FI2

29) chain C
residue 276
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168
source Swiss-Prot : SWS_FT_FI2

30) chain C
residue 190
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168
source Swiss-Prot : SWS_FT_FI3

31) chain C
residue 240
type BINDING
sequence H
description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I
source Swiss-Prot : SWS_FT_FI4

32) chain C
residue 306
type BINDING
sequence C
description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I
source Swiss-Prot : SWS_FT_FI4

33) chain C
residue 308
type BINDING
sequence C
description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I
source Swiss-Prot : SWS_FT_FI4

34) chain C
residue 234
type BINDING
sequence C
description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I
source Swiss-Prot : SWS_FT_FI4


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