eF-site ID 5wj6-ABCD
PDB Code 5wj6
Chain A, B, C, D

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Title Crystal structure of glutaminase C in complex with inhibitor 2-phenyl-N-{5-[4-({5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}amino)piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide (UPGL-00004)
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Glutaminase kidney isoform, mitochondrial
Source (GLSK_HUMAN)
Sequence A:  PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLK
ECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFR
RKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKF
SPDLWGVSVCTADGQRHSTGDTKVPFCLQSCVKPLKYAIA
VNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNA
TFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQ
LCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNT
LSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVM
GMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREG
B:  PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLK
ECMDMLRLTLQTTSDGVMLDKDLFKKCVNSNIVLLTQAFR
RKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKF
SPDLWGVSVCTADGQRHSTGDTKVPFCLQSCVKPLKYAIA
VNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNA
TFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQ
LCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNT
LSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVM
GMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREG
C:  PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLK
ECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFR
RKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKF
SPDLWGVSVCTADGQRHSTGDTKVPFCLQSCVKPLKYAIA
VNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNA
TFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQ
LCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNT
LSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVM
GMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREG
D:  PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLK
ECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFR
RKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKF
SPDLWGVSVCTADGQRHSTGDTKVPFCLQSCVKPLKYAIA
VNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNA
TFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQ
LCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNT
LSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVM
GMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREG
Description


Functional site
1) chain A
residue 317
type
sequence R
description binding site for residue B4A A 601
source : AC1
2) chain A
residue 320
type
sequence K
description binding site for residue B4A A 601
source : AC1
3) chain A
residue 321
type
sequence L
description binding site for residue B4A A 601
source : AC1
4) chain A
residue 322
type
sequence F
description binding site for residue B4A A 601
source : AC1
5) chain A
residue 323
type
sequence L
description binding site for residue B4A A 601
source : AC1
6) chain A
residue 324
type
sequence N
description binding site for residue B4A A 601
source : AC1
7) chain A
residue 325
type
sequence E
description binding site for residue B4A A 601
source : AC1
8) chain A
residue 394
type
sequence Y
description binding site for residue B4A A 601
source : AC1
9) chain B
residue 317
type
sequence R
description binding site for residue B4A A 601
source : AC1
10) chain D
residue 320
type
sequence K
description binding site for residue B4A A 601
source : AC1
11) chain D
residue 321
type
sequence L
description binding site for residue B4A A 601
source : AC1
12) chain D
residue 322
type
sequence F
description binding site for residue B4A A 601
source : AC1
13) chain D
residue 323
type
sequence L
description binding site for residue B4A A 601
source : AC1
14) chain D
residue 324
type
sequence N
description binding site for residue B4A A 601
source : AC1
15) chain D
residue 325
type
sequence E
description binding site for residue B4A A 601
source : AC1
16) chain D
residue 394
type
sequence Y
description binding site for residue B4A A 601
source : AC1
17) chain A
residue 317
type
sequence R
description binding site for residue B4A C 601
source : AC2
18) chain B
residue 320
type
sequence K
description binding site for residue B4A C 601
source : AC2
19) chain B
residue 321
type
sequence L
description binding site for residue B4A C 601
source : AC2
20) chain B
residue 322
type
sequence F
description binding site for residue B4A C 601
source : AC2
21) chain B
residue 323
type
sequence L
description binding site for residue B4A C 601
source : AC2
22) chain B
residue 324
type
sequence N
description binding site for residue B4A C 601
source : AC2
23) chain B
residue 325
type
sequence E
description binding site for residue B4A C 601
source : AC2
24) chain B
residue 394
type
sequence Y
description binding site for residue B4A C 601
source : AC2
25) chain C
residue 320
type
sequence K
description binding site for residue B4A C 601
source : AC2
26) chain C
residue 321
type
sequence L
description binding site for residue B4A C 601
source : AC2
27) chain C
residue 322
type
sequence F
description binding site for residue B4A C 601
source : AC2
28) chain C
residue 323
type
sequence L
description binding site for residue B4A C 601
source : AC2
29) chain C
residue 324
type
sequence N
description binding site for residue B4A C 601
source : AC2
30) chain C
residue 325
type
sequence E
description binding site for residue B4A C 601
source : AC2
31) chain C
residue 394
type
sequence Y
description binding site for residue B4A C 601
source : AC2
32) chain B
residue 388
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI2
33) chain C
residue 388
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI2
34) chain D
residue 388
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI2
35) chain C
residue 164
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3
source Swiss-Prot : SWS_FT_FI4
36) chain D
residue 164
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3
source Swiss-Prot : SWS_FT_FI4
37) chain B
residue 164
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3
source Swiss-Prot : SWS_FT_FI4
38) chain C
residue 311
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
39) chain D
residue 311
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
40) chain B
residue 311
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5
41) chain D
residue 414
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
42) chain D
residue 466
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
43) chain D
residue 484
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
44) chain C
residue 466
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
45) chain C
residue 484
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
46) chain D
residue 286
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
47) chain D
residue 335
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
48) chain D
residue 381
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
49) chain B
residue 484
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
50) chain C
residue 286
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
51) chain C
residue 335
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
52) chain C
residue 381
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
53) chain B
residue 286
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
54) chain B
residue 335
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
55) chain B
residue 381
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
56) chain B
residue 414
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
57) chain B
residue 466
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1
58) chain C
residue 414
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1
source Swiss-Prot : SWS_FT_FI1

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