eF-site ID 5wj6-B
PDB Code 5wj6
Chain B

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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 B:  PSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLK
ECMDMLRLTLQTTSDGVMLDKDLFKKCVNSNIVLLTQAFR
RKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKF
SPDLWGVSVCTADGQRHSTGDTKVPFCLQSCVKPLKYAIA
VNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNA
GAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNA
TFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQ
LCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNT
LSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVM
GMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHF
AKKLDPRREG
Description


Functional site

1) chain B
residue 317
type
sequence R
description binding site for residue B4A A 601
source : AC1

2) chain B
residue 320
type
sequence K
description binding site for residue B4A C 601
source : AC2

3) chain B
residue 321
type
sequence L
description binding site for residue B4A C 601
source : AC2

4) chain B
residue 322
type
sequence F
description binding site for residue B4A C 601
source : AC2

5) chain B
residue 323
type
sequence L
description binding site for residue B4A C 601
source : AC2

6) chain B
residue 324
type
sequence N
description binding site for residue B4A C 601
source : AC2

7) chain B
residue 325
type
sequence E
description binding site for residue B4A C 601
source : AC2

8) chain B
residue 394
type
sequence Y
description binding site for residue B4A C 601
source : AC2

9) 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

10) 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

11) 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

12) 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

13) 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

14) 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

15) 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

16) chain B
residue 164
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3
source Swiss-Prot : SWS_FT_FI4

17) chain B
residue 311
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5


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