eF-site ID 4ejx-D
PDB Code 4ejx
Chain D

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Title Structure of ceruloplasmin-myeloperoxidase complex
Classification OXIDOREDUCTASE
Compound Ceruloplasmin
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence D:  VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPA
CPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSN
QLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPC
FLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWD
GERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQP
MEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLN
RQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPG
YNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPN
NIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIF
MSNSYPRDFVNCSTLPALNLASWREA
Description


Functional site

1) chain D
residue 239
type catalytic
sequence R
description 601
source MCSA : MCSA1

2) chain D
residue 242-252
type prosite
sequence EMPELTSMHTL
description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
source prosite : PS00435

3) chain D
residue 168
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 170
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
source Swiss-Prot : SWS_FT_FI1

5) chain D
residue 172
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
source Swiss-Prot : SWS_FT_FI1

6) chain D
residue 174
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
source Swiss-Prot : SWS_FT_FI1

7) chain D
residue 242
type BINDING
sequence E
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2

8) chain D
residue 243
type BINDING
sequence M
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2

9) chain D
residue 336
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3

10) chain D
residue 239
type SITE
sequence R
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4

11) chain D
residue 150
type MOD_RES
sequence C
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5

12) chain D
residue 157
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
source Swiss-Prot : SWS_FT_FI6

13) chain D
residue 189
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI7

14) chain D
residue 225
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI7

15) chain D
residue 317
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI8

16) chain D
residue 563
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087
source Swiss-Prot : SWS_FT_FI9


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