eF-site ID 1y8n-AB
PDB Code 1y8n
Chain A, B

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Title Crystal structure of the PDK3-L2 complex
Classification TRANSFERASE
Compound [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3
Source Homo sapiens (Human) (ODP2_HUMAN)
Sequence A:  PKQIERYSRFSPSPLSIKQFLDFGRDNACEKTSYMFLRKE
LPVRLANTMREVNLLPDNLLNRPSVGLVQSWYMQSFLELL
EYENKSPEDPQVLDNFLQVLIKVRNRHNDVVPTMAQGVIE
YKEKFGFDPFISTNIQYFLDRFYTNRISFRMLINQHTLLF
GGDTNPVHPKHIGSIDPTCNVADVVKDAYETAKMLCEQYY
LVAPELEVEEFNAKAPDKPIQVVYVPSHLFHMLFELFKNS
MRATVELYEDRKEGYPAVKTLVTLGKEDLSIKISDLGGGV
PLRKIDRLFNYMYSPLFGYGLPISRLYARYFQGDLKLYSM
EGVGTDAVIYLKALSSESFERLPVFNKSAWRHYKTTPEAD
DWSNPSSEPRDASK
B:  SYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLA
EIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCII
VEKEADISAFADYTDLK
Description


Functional site

1) chain A
residue 20
type
sequence S
description BINDING SITE FOR RESIDUE K A 501
source : AC1

2) chain A
residue 21
type
sequence R
description BINDING SITE FOR RESIDUE K A 501
source : AC1

3) chain A
residue 22
type
sequence F
description BINDING SITE FOR RESIDUE K A 501
source : AC1

4) chain A
residue 59
type
sequence N
description BINDING SITE FOR RESIDUE K A 501
source : AC1

5) chain A
residue 372
type
sequence F
description BINDING SITE FOR RESIDUE K A 501
source : AC1

6) chain A
residue 48
type
sequence F
description BINDING SITE FOR RESIDUE RED B 373
source : AC2

7) chain B
residue 173
type
sequence K
description BINDING SITE FOR RESIDUE RED B 373
source : AC2

8) chain A
residue 278
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q922H2
source Swiss-Prot : SWS_FT_FI2

9) chain B
residue 138-149
type prosite
sequence PALSPTMTMGTV
description AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV
source prosite : PS00178

10) chain B
residue 157-186
type prosite
sequence GEKLSEGDLLAEIETDKATIGFEVQEEGYL
description LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GekLsegDLLaeIETdKATigFevqeeGyL
source prosite : PS00189

11) chain B
residue 206
type MOD_RES
sequence I
description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 287
type MOD_RES
sequence D
description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 306
type MOD_RES
sequence S
description N6-lipoyllysine => ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000269|PubMed:15861126, ECO:0000269|PubMed:17532006, ECO:0000269|PubMed:17683942, ECO:0000269|PubMed:25525879, ECO:0007744|PDB:1Y8N, ECO:0007744|PDB:1Y8O, ECO:0007744|PDB:1Y8P, ECO:0007744|PDB:2PNR, ECO:0007744|PDB:2Q8I
source Swiss-Prot : SWS_FT_FI1


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